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2-Bromo-1-chloro-4-trifluoromethoxybenzene
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2-Bromo-1-chloro-4-trifluoromethoxybenzene
Catalog Number:
(103404-602)
Supplier:
Novus Biologicals
Description:
The Bcl-xL Antibody (BX006) [Biotin] from Novus Biologicals is a mouse monoclonal antibody to Bcl-xL. This antibody reacts with human, mouse, rat, porcine. The Bcl-xL Antibody (BX006) [Biotin] has been validated for the following applications: Western Blot, Flow Cytometry, ELISA, Immunocytochemistry / Immunofluorescence, Immunoprecipitation, Immunohistochemistry-Paraffin, Immunohistochemistry-Frozen.
Catalog Number:
(103404-570)
Supplier:
Novus Biologicals
Description:
The Bcl-2 Antibody (SPM530) [PerCP] from Novus Biologicals is a mouse monoclonal antibody to Bcl-2. This antibody reacts with human, mouse (negative), rat (negative). The Bcl-2 Antibody (SPM530) [PerCP] has been validated for the following applications: Western Blot, Flow Cytometry, Immunocytochemistry / Immunofluorescence, Immunoprecipitation, Immunohistochemistry-Paraffin, Immunohistochemistry-Frozen.
Supplier:
AMBEED, INC
Description:
(R)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)(methyl)amino)pentanoic acid, Purity: 95%, CAS Number: 1799443-42-7, Appearance: Solid, Storage: Sealed in dry, 2-8 C, Size: 1g
Catalog Number:
(103404-336)
Supplier:
Novus Biologicals
Description:
The Bax Antibody (SPM336) [HRP] from Novus Biologicals is a mouse monoclonal antibody to Bax. This antibody reacts with human, primate, mouse (negative), rat (negative). The Bax Antibody (SPM336) [HRP] has been validated for the following applications: Western Blot, Flow Cytometry, ELISA, Immunocytochemistry / Immunofluorescence, Immunoprecipitation, Immunohistochemistry-Paraffin, Immunohistochemistry-Frozen.
Catalog Number:
(TCF0872-25G)
Supplier:
TCI America
Description:
CAS Number: 35661-51-9
MDL Number: MFCD00239419 Molecular Formula: C15H14N2O2 Molecular Weight: 254.29 Purity/Analysis Method: >98.0% (HPLC,T) Form: Crystal Melting point (°C): 171 Storage Temperature: 0-10°C
Catalog Number:
(D-2125.0001BA)
Supplier:
Bachem Americas
Description:
Useful for the synthesis of peptide amides using Fmoc strategy. Cleavage has been performed with 50 % TFA in CH₂Cl₂ or 95% aqueous TFA. Scavengers may be required.
Catalog Number:
(10425-208)
Supplier:
Bioss
Description:
ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilization. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.
Catalog Number:
(10425-186)
Supplier:
Bioss
Description:
ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilization. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.
Catalog Number:
(10425-200)
Supplier:
Bioss
Description:
ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilization. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.
Catalog Number:
(10425-198)
Supplier:
Bioss
Description:
ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilization. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.
Catalog Number:
(76081-304)
Supplier:
Bioss
Description:
ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilization. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.
Supplier:
AMBEED, INC
Description:
(S)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)-3-(2,5-dichlorophenyl)propanoic acid 97%
Supplier:
AMBEED, INC
Description:
(S)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)(methyl)amino)-4-methoxy-4-oxobutanoic acid, Purity: 97%, CAS Number: 2044710-58-7, Appearance: Solid, Storage: Sealed in dry, 2-8 C, Size: 1g
Supplier:
AMBEED, INC
Description:
(R)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)hept-6-enoic acid, Purity: 98%, CAS Number: 1093645-21-6, Appearance: White to Yellow Solid, Storage: Sealed in dry, 2-8C, Size: 250MG
Supplier:
AMBEED, INC
Description:
(R)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)-3-(2-methyl-1H-indol-3-yl)propanoic acid, Purity: 95%, CAS number: 196808-79-4, Appearance: Solid, Storage: Sealed in dry, 2-8C, Size: 250MG
Catalog Number:
(B-3930.0005BA)
Supplier:
Bachem Americas
Description:
These dipeptide building blocks containing Ser- or Thr-derived oxazolidines (pseudoprolines) proved to be versatile tools for overcoming some intrinsic problems in the field of peptide chemistry. The presence of pseudoprolines within a peptide sequence results in the disruption of β-sheet structures considered as a source of intermolecular aggregation during chain elongation, thus increasing solvation and coupling kinetics in peptide assembly. Therefore, use of pseudoprolines offer new possibilities for accessing large peptides by convergent strategies and chemoselective ligation techniques. Moreover, incorporation of a pseudoproline unit facilitates cyclization of peptides.
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 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
is still displayed and you need assistance, please call us at 1-800-932-5000.
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