Human Adducin 2 (ADD2) activation kit by CRISPRa

CAT#: GA100081

ADD2 CRISPRa kit - CRISPR gene activation of human adducin 2

Product Images

Specifications

Product Data

• Format: 3gRNAs, 1 scramble ctrl and 1 enhancer vector
• Symbol: ADD2
• Locus ID: 119
• Kit Components:

  GA100081G1, Adducin 2 gRNA vector 1 in pCas-Guide-GFP-CRISPRa

  GA100081G2, Adducin 2 gRNA vector 2 in pCas-Guide-GFP-CRISPRa

  GA100081G3, Adducin 2 gRNA vector 3 in pCas-Guide-GFP-CRISPRa

  1 CRISPRa-Enhancer vector, SKU GE100056

  1 CRISPRa scramble vector, SKU GE100077

• Disclaimer: The kit is designed based on the best knowledge of CRISPa SAM technology. The efficiency of the activation can be affected by many factors, including nucleosome occupancy status, chromatin structure and the gene expression level of the target, etc.

Reference Data

• RefSeq: NM_001185054, NM_001185055, NM_001617, NM_017482, NM_017483, NM_017484, NM_017485, NM_017486, NM_017487, NM_017488, N53078
• Synonyms: ADDB
• Summary: 'Adducins are heteromeric proteins composed of different subunits referred to as adducin alpha, beta and gamma. The three subunits are encoded by distinct genes and belong to a family of membrane skeletal proteins involved in the assembly of spectrin-actin network in erythrocytes and at sites of cell-cell contact in epithelial tissues. While adducins alpha and gamma are ubiquitously expressed, the expression of adducin beta is restricted to brain and hematopoietic tissues. Adducin, originally purified from human erythrocytes, was found to be a heterodimer of adducins alpha and beta. Polymorphisms resulting in amino acid substitutions in these two subunits have been associated with the regulation of blood pressure in an animal model of hypertension. Heterodimers consisting of alpha and gamma subunits have also been described. Structurally, each subunit is comprised of two distinct domains. The amino-terminal region is protease resistant and globular in shape, while the carboxy-terminal region is protease sensitive. The latter contains multiple phosphorylation sites for protein kinase C, the binding site for calmodulin, and is required for association with spectrin and actin. Alternatively spliced transcript variants have been described. [provided by RefSeq, Jun 2010]'