Keep my session open?
Ending In 
The session is expired
Your session has expired. For your security, we have logged you out.
Would you like to log in again?

Update to Avantor’s response to the coronavirus (COVID-19) pandemic

  • Product Results
  • Product Category
  • Criteria
  • Supplier
  • Refine by Suppliers
    Sort by:

  • Search Within Results

You Searched For:

2-Amino-4-bromo-5-fluorobenzoic+acid


38,221  results were found

SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-SearchPresentationType-HORIZONTAL
 
 
SearchResultCount:"38221"
  List View Searching Easy View BETA(new)
Sort by:
 
 
 
 


Supplier:  Bioss
Description:   Protein kinases are enzymes that transfer a phosphate group from a phosphate donor onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. The protein kinase family is one of the largest families of proteins in eukaryotes, classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains. Epidermal Growth factor receptor (EGFR) is the prototype member of the type 1 receptor tyrosine kinases. EGFR overexpression in tumors indicates poor prognosis and is observed in tumors of the head and neck, brain, bladder, stomach, breast, lung, endometrium, cervix, vulva, ovary, esophagus, stomach and in squamous cell carcinoma.

Supplier:  Bioss
Description:   Protein kinases are enzymes that transfer a phosphate group from a phosphate donor onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. The protein kinase family is one of the largest families of proteins in eukaryotes, classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains. Epidermal Growth factor receptor (EGFR) is the prototype member of the type 1 receptor tyrosine kinases. EGFR overexpression in tumors indicates poor prognosis and is observed in tumors of the head and neck, brain, bladder, stomach, breast, lung, endometrium, cervix, vulva, ovary, esophagus, stomach and in squamous cell carcinoma.
Supplier:  Bioss
Description:   Catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. Also acts on D-erythro-dihydrosphingosine, D-erythro-sphingosine and L-threo-dihydrosphingosine. Binds phosphoinositides.

Supplier:  Bioss
Description:   Catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. Also acts on D-erythro-dihydrosphingosine, D-erythro-sphingosine and L-threo-dihydrosphingosine. Binds phosphoinositides.
Supplier:  Bioss
Description:   Hemidesmosomes are structures which link the basal lamina to the intermediate filament cytoskeleton. An important functional component of hemidesmosomes is the integrin beta-4 subunit (ITGB4), a protein containing two fibronectin type III domains. The protein encoded by Intergrin beta 4 binding protein binds to the fibronectin type III domains of ITGB4 and may help link ITGB4 to the intermediate filament cytoskeleton. The encoded protein, which is insoluble and found both in the nucleus and in the cytoplasm, can function as a translation initiation factor and prevent the association of the 40S and 60S ribosomal subunits. Multiple transcript variants encoding several different isoforms have been found for this gene.
Supplier:  AMBEED, INC
Description:   1,2-Distearoyl-sn-glycero-3-phosphoethanolamine 95%
Supplier:  Bioss
Description:   UGP2 (UDP glucose pyrophosphorylase 2) is an important intermediary in cellular metabolic pathways. It transfers a glucose moiety from glucose-1-phosphate to MgUTP and forms UDP glucose and MgPPi.
Supplier:  Bioss
Description:   Protein kinases are enzymes that transfer a phosphate group from a phosphate donor onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. The protein kinase family is one of the largest families of proteins in eukaryotes, classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains. Epidermal Growth factor receptor (EGFR) is the prototype member of the type 1 receptor tyrosine kinases. EGFR overexpression in tumors indicates poor prognosis and is observed in tumors of the head and neck, brain, bladder, stomach, breast, lung, endometrium, cervix, vulva, ovary, esophagus, stomach and in squamous cell carcinoma.

Supplier:  Bioss
Description:   Protein kinases are enzymes that transfer a phosphate group from a phosphate donor onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. The protein kinase family is one of the largest families of proteins in eukaryotes, classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains. Epidermal Growth factor receptor (EGFR) is the prototype member of the type 1 receptor tyrosine kinases. EGFR overexpression in tumors indicates poor prognosis and is observed in tumors of the head and neck, brain, bladder, stomach, breast, lung, endometrium, cervix, vulva, ovary, esophagus, stomach and in squamous cell carcinoma.

Supplier:  Bioss
Description:   Protein kinases are enzymes that transfer a phosphate group from a phosphate donor onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. The protein kinase family is one of the largest families of proteins in eukaryotes, classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains. Epidermal Growth factor receptor (EGFR) is the prototype member of the type 1 receptor tyrosine kinases. EGFR overexpression in tumors indicates poor prognosis and is observed in tumors of the head and neck, brain, bladder, stomach, breast, lung, endometrium, cervix, vulva, ovary, esophagus, stomach and in squamous cell carcinoma.
Supplier:  Veltek Associates
Description:   Dec-Quat 200V is a neutral pH quaternary ammonium solution It is phosphate free, non-sterile and an EPA registered disinfectant, virucide, sanitizer, germicidal detergent, deodorant and fungicide designed specifically for the life science and research and development industries.
MSDS SDS

Supplier:  Biotium
Description:   This MAb recognizes a protein of 165 kDa, identified as carbamoyl phosphate synthetase 1 (CPS1). This mitochondrial enzyme catalyzes synthesis of carbamoyl phosphate from ammonia and bicarbonate. This reaction is the first committed step of the urea cycle, which is important in the removal of excess urea from cells.Deficiency of CPS1 is an autosomal recessive disorder that causes hyperammonemia. CPS1 is a hepatocyte specific protein that localizes to the mitochondria of hepatocytes. It is a sensitive marker for distinguishing hepatocellular carcinomas (HCC) from other metastatic carcinomas as well as cholangio-carcinomas. HCC s occur primarily in the stomach, but they are also found in many other organs. CPS1 may also be a useful marker for intestinal metaplasia. Reportedly, strong expression of CPS1 correlates with smaller tumor size and longer patient survival. Occasionally, CPS1 is also found in gastric carcinomas as well as in a few other non-hepatic tumors.
Supplier:  Bioss
Description:   Binds phospholipids; exhibits strong binding to phosphatidic acid and weak binding to phosphatidylinositol 3-phosphate (By similarity). Stabilizes GTP-bound RAB7A on late endosomes/lysosomes and alters functional properties of late endocytic compartments via its interaction with RAB7A.
Catalog Number: (76071-160)

Supplier:  Prosci
Description:   TPI1, Polyclonal Antibody, Host: Rabbit, Species: Human, Mouse, Immunogen: conjugated synthetic peptide between 258-286 amino acids from the C-terminal region, Isotype: Ig, Synonym: Triosephosphate isomerase, TIM, Triose-phosphate isomeras
Supplier:  MP Biomedicals
Description:   Lyophilized from 0.02M Ammonium Bicarbonate (may contain traces of buffer salt).
Immunological identity verified by radial immunodiffusion. Cellulose acetate electrophoresis shows one band indicating β2 electrophoretic mobility. SDS-PAGE shows one band corresponding to a molecular weight of approximately 12,000.
Reconstitution: To reconstitute use a phosphate buffer, pH >7.0, containing 0.15 M NaCl.

Supplier:  Bioss
Description:   Matrix Metalloproteinase 8 (MMP8) is also known as neutrophil collagenase and collagenase 2. MMP8 degrades fibrillar collagens types I, II, III, aggrecan, serpins and alpha 2 macroglobulin. All collagenases cleave fibrillar collagens at one specific site resulting in generation of N terminal three quarter and C terminal one quarter fragments, which then denature to gelatin at body temperature. The substrate specificity of collagenases is variable: MMP1 degrades type III collagen more efficiently than type I or type II collagen, whereas MMP8 is more potent in degrading type I collagen than type III or type II collagen. MMP13, in turn degrades type II collagen 6 fold more efficiently than type I and type II collagens and displays almost 50 fold stronger gelatinolytic activity than MMP1 and MMP8. MMP8 is very similar to MMP1, sharing 57 % amino acid identity. Most cell types do not produce MMP8. Until recently, it was thought that MMP8 was produced exclusively by neutrophils, but it has also been detected in other cell types including arthritic chondrocytes and gingival fibroblasts. The human MMP8 gene has the chromosomal location of 11q22.2-22.3. MMP8 is heavily glycosylated, and the zymogen has a mass of 85 Kd. The zymogen is quickly activated to the 64 Kd form, and this breaks down to a cascade of active forms.
Inquire for Price
Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us at 1-800-932-5000.
Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us at 1-800-932-5000.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at Regulatory_Affairs@vwr.com
-Additional Documentation May be needed to purchase this item. A VWR representative will contact you if needed.
This product has been blocked by your organization. Please contact your purchasing department for more information.
The original product is no longer available. The replacement shown is available.
This product is no longer available. Alternatives may be available by searching with the VWR Catalog Number listed above. If you need further assistance, please call VWR Customer Service at 1-800-932-5000.
5,825 - 5,840  of 38,221