Dynein light chain 2, cytoplasmic Rabbit pAb (一抗) | Bioss

bs-14469R

宠物抗体、农牧业/家禽抗体

Dynein light chain 2, cytoplasmic Rabbit pAb

胞浆动力蛋白轻链2抗体

DNCL1B; Dlc2; RSPH22; 1700064A15Rik; 6720463E02Rik; DLC8; DLC8b; DYL2_HUMAN; DYNLL2; 8 kDa dynein light chain b (DLC8b); Dynein light chain LC8-type 2; DYL2_MOUSE; 8 kDa dynein light chain b (DLC8 | DLC8b); DYL2_RAT;

Rabbit

KLH conjugated synthetic peptide derived from human Dynein light chain 2: 1-89/89

IgG

Liquid

affinity purified by Protein A

Polyclonal

10 kDa

1mg/ml

0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Shipped at 4℃. Store at -20℃ for one year. Avoid repeated freeze/thaw cycles.

This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.

Dyneins are multisubunit, high molecular weight ATPases that interact with microtubules to generate force by converting the chemical energy of ATP into the mechanical energy of movement. Cytoplasmic or axonemal Dynein heavy, intermediate, light and light-intermediate chains are all components of minus end-directed motors; the complex transports cellular cargos towards the central region of the cell. The highly conserved DYNLL proteins were originally identified as light chains for microtubule-based motor protein Dynein. In mammals there are two closely related isoforms expressed, DYNLL1 and DYNLL2 which share 93% sequence identity at the protein level. DYNLL1 (Dynein light chain 1) also designated, DLC8 or PIN (Protein inhibitor of neuronal nitric oxide synthase) has been identified as a protein that interacts with NOS1 resulting in NOS1 inhibition. Dimerization is required for NOS1 activity and DYNLL1 has been shown to destabilize the NOS1 dimer. Nitric oxide may be involved in several processes such as apoptosis, synaptogenesis and neuronal development; thus DYNLL1 is implicated in these processes as well. DYNLL1 is a ubiquitously expressed protein that exhibits high expression in testis and moderate expression in brain. DYNLL2 (Dynein light chain 2) is subject to a unique alternative splicing event which is implicated in Myosin Va binding specificity.