Crystallin, gamma D (CRYGD) (AA 75-175) antibody

Details for Product No. ABIN393234
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Antigen
Synonyms ccp, caca, cca3, cryg4, cry-g-d, MGC85594, CRYGD, CACA, CCA3, CCP, CRYG4, CTRCT4, PCC, cry-g-D, Aey4, Cryg-1, DGcry-1, Lop12, Cryg4, Len
Epitope
AA 75-175
(7), (7), (6), (3), (3), (2), (2), (1)
Reactivity
Human
(28), (12)
Host
Mouse
(28), (12)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(3), (3), (3), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Western Blotting (WB)
(29), (20), (10), (3), (3), (3), (1)
Pubmed 5 references available
Quantity 0.1 mg
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Catalog No. ABIN393234
450.00 $
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Immunogen CRYGD (NP_008822, 75 a.a. ~ 175 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 K
Clone 4E12
Isotype IgG1 kappa
Specificity CRYGD (NP_008822, 75 a.a. ~ 175 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Purification This antibody is purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS.
Alternative Name CRYGD
Background Synonyms: Serine protease inhibitor J6, 47 kDa heat shock protein, Collagen-binding protein, Colligin, Serpin H1,Hsp47, Cbp1, Serpinh1
Molecular Weight 20738 DA
Gene ID 12406
NCBI Accession NP_008822
Research Area Neurology, Cell Structure
Application Notes Western blot = 1:500-1000
Comment

Background: Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families, beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. Four gamma-crystallin genes (gamma-A through gamma-D) and three pseudogenes (gamma-E, gamma-F, gamma-G) are tandemly organized in a genomic segment as a gene cluster. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.

Restrictions For Research Use only
Buffer PBS with 0.09% (w/v) sodium azide.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage 4 °C/-20 °C
Storage Comment Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles
Expiry Date 6 months
Supplier Images
anti-Crystallin, gamma D (CRYGD) (AA 75-175) antibody CRYGD monoclonal antibody (M03), clone 4E12 Western Blot analysis of CRYGD expression in HepG2. Detection limit for recombinant GST tagged CRYGD is approximately 0.03 ng/mL as a capture antibody.
anti-Crystallin, gamma D (CRYGD) (AA 75-175) antibody (2) anti-Crystallin, gamma D (CRYGD) (AA 75-175) antibody (Image 2)
Background publications Moreau, King: "Hydrophobic core mutations associated with cataract development in mice destabilize human gammaD-crystallin." in: The Journal of biological chemistry, Vol. 284, Issue 48, pp. 33285-95, 2009 (PubMed).

Das, King, Zhou: "beta-Strand interactions at the domain interface critical for the stability of human lens gammaD-crystallin." in: Protein science : a publication of the Protein Society, Vol. 19, Issue 1, pp. 131-40, 2010 (PubMed).

Roshan, Vijaya, Lavanya et al.: "A novel human CRYGD mutation in a juvenile autosomal dominant cataract." in: Molecular vision, Vol. 16, pp. 887-96, 2010 (PubMed).

Pande, Ghosh, Banerjee et al.: "Increase in surface hydrophobicity of the cataract-associated P23T mutant of human gammaD-crystallin is responsible for its dramatically lower, retrograde solubility." in: Biochemistry, Vol. 49, Issue 29, pp. 6122-9, 2010 (PubMed).

Acosta-Sampson, King: "Partially folded aggregation intermediates of human gammaD-, gammaC-, and gammaS-crystallin are recognized and bound by human alphaB-crystallin chaperone." in: Journal of molecular biology, Vol. 401, Issue 1, pp. 134-52, 2010 (PubMed).

Validation Images
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