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CRYGA Rabbit pAb

Cat No.: DPA03622
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Product Name: CRYGA Rabbit pAb
Cat No.: DPA03622
Clonality: Polyclonal
Species Reactivity: Human, Mouse, Rat
Tested Applications: WB
Recommended Dilution: WB: 1:1000
Size: 30ul 50ul 100uL
Format: Liquid
Source: Rabbit
Purification Method: Affinity Purification
Isotype: IgG
Conjugate: Un-conjugated
Storage: Store at -20°C. Supplied in 50nM Tris-Glycine(pH 7.4), 0.15M NaCl, 40%Glycerol, 0.01% sodium azide a
Immunogen: Recombinant protein of human CRYGA
Calculated Molecular Weight: 21 kDa
Observed Molecular Weight: 21 kDa
GenBank Accession Number: P11844
Gene ID (NCBI): 1418
Synonyms: CRYG1; CRYG5; CRY-g-A
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. [provided by RefSeq, Jul 2008]
Category: Primary Ab
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