CRYBA1 anticorps (N-Term)

N° du produit ABIN630602

L’anticorps Lapin Polyclonal anti-CRYBA1 a été validé pour WB. Il convient pour détecter CRYBA1 dans des échantillons de Humain, Souris et Rat.

Aperçu rapide pour CRYBA1 anticorps (N-Term) (ABIN630602)

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

Reactivité: Humain, Souris, Rat

Hôte: Lapin

Clonalité: Polyclonal

Conjugué: Cet anticorp CRYBA1 est non-conjugé

Application: Western Blotting (WB)

Détail du produit anti-CRYBA1 anticorps

Épitope: N-Term

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

Purification: Affinity purified

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

Information d'application

Indications d'application: WB: 1 µg/mL
Optimal conditions should be determined by the investigator.

Commentaires:

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

Stockage

Format: Lyophilized

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

Concentration: Lot specific

Buffer: PBS

Conseil sur la manipulation: Avoid repeated freeze/thaw cycles.
Dilute only prior to immediate use.

Stock: 4 °C/-20 °C

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

Détails sur CRYBA1

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

Autre désignation: Crystallin beta A1

Sujet: 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.

Poids moléculaire: 25 kDa (MW of target protein)