CRYBA1 antibody (N-Term)

Catalog No. ABIN630602

The Rabbit Polyclonal anti-CRYBA1 antibody has been validated for WB. It is suitable to detect CRYBA1 in samples from Human, Mouse and Rat.

Quick Overview for CRYBA1 antibody (N-Term) (ABIN630602)

Target: CRYBA1 (Crystallin, beta A1 (CRYBA1))

Reactivity: Human, Mouse, Rat

Host: Rabbit

Clonality: Polyclonal

Conjugate: This CRYBA1 antibody is un-conjugated

Application: Western Blotting (WB)

Product Details anti-CRYBA1 Antibody

Binding Specificity: N-Term

Specificity: Crystallin Beta A1 antibody was raised against the N terminal of CRYBA1

Purification: Affinity purified

Immunogen: Crystallin Beta A1 antibody was raised using the N terminal of CRYBA1 corresponding to a region with amino acids METQAEQQELETLPTTKMAQTNPTPGSLGPWKITIYDQENFQGKRMEFTS

Application Details

Application Notes: WB: 1 µg/mL
Optimal conditions should be determined by the investigator.

Comment:

Crystallin Beta A1 Blocking Peptide, (ABIN5613010), is also available for use as a blocking control in assays to test for specificity of this Crystallin Beta A1 antibody

Restrictions: For Research Use only

Handling

Format: Lyophilized

Reconstitution: Lyophilized powder. Add distilled water for a 1 mg/mL concentration of CRYBA1 antibody in PBS

Concentration: Lot specific

Buffer: PBS

Handling Advice: Avoid repeated freeze/thaw cycles.
Dilute only prior to immediate use.

Storage: 4 °C/-20 °C

Storage Comment: Store at 2-8 °C for short periods. For longer periods of storage, store at -20 °C.

Target Details for CRYBA1

Target: CRYBA1 (Crystallin, beta A1 (CRYBA1))

Alternative Name: Crystallin beta A1

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-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins.

Molecular Weight: 25 kDa (MW of target protein)