Recombinant Rat Claudin-5 (CLDN5) Protein (His)

Name: Recombinant Rat Claudin-5 (CLDN5) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07932P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Rat Claudin-5 (CLDN5) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Activity	Not tested.
Uniprotkb	Q9JKD6
Target Symbol	CLDN5
Species	Rattus norvegicus (Rat)
Expression System	in vitro E.coli expression system
Tag	N-10His
Target Protein Sequence	MGSAALEILGLVLCLVGWVGLILACGLPMWQVTAFLDHNIVTAQTTWKGLWMSCVVQSTGHMQCKVYESVLALSAEVQAARALTVGAVLLALVALFVTLTGAQCTTCVAPGPVKARVALTGGALYALCGLLALVPLCWFANIVVREFYDPTVPVSQKYELGAALYIGWAASALLMCGGGLVCCGAWVCTGRPEFSFPVKYSAPRRTTANGDYDKKNYV
Expression Range	1-218aa
Protein Length	Full Length
Mol. Weight	24.6 kDa
Research Area	Neuroscience
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Plays a major role in tight junction-specific obliteration of the intercellular space.
Subcellular Location	Cell junction, tight junction. Cell membrane; Multi-pass membrane protein.
Protein Families	Claudin family
Database References	KEGG: rno:65131 STRING: 10116.ENSRNOP00000064048 UniGene: PMID: 28741371 in response to alcohol, increased claudin-5 paradoxically accompanies an increase in paracellular leak and rearrangement of alveolar tight junctions. PMID: 27452368 Immunocytochemistry and Western blotting showed that claudin-5, a critical regulatory protein for tight junctions, was translocated from the membrane to the cytoplasm after cooling in cultured bEnd3 cells PMID: 23653089 Increased claudin-5 and claudin-1 expression and decreased permeability of the blood brain barrier were observed in the hyperbaric oxygenation and cerebral ischemia-reperfusion injury group. PMID: 21626096 Claudin-5 redistribution, mediated by caveolin-1, was observed in blood brain barrier following ischemic stroke. PMID: 22378877 Levels of tight junction protein claudin 5 are decreased in blood-brain barrier cells post-translationally following neurotoxicant administration. PMID: 20970449 Blood-brain barrier permeability increases after stroke through matrix metalloprotein-mediated degradation of claudin-5 and occuludin in tight junctions. PMID: 21717368 Data demonstrate the timing of tight junction-associated proteins claudin-5, occludin, and ZO-1 in light of blood-brain barrier permeability associated with cerebral ischemia reperfusion. PMID: 21318404 These findings suggest that claudin-5 is a main claudin expressed in podocytes and that the formation of tight junctions in the nephrosis may be due to local recruitment of claudin-5 rather than due to total upregulation of the claudin protein levels. PMID: 21271259 claudin-5 and occludin translocate reversibly within cells of the rat blood-optic nerve barrier after borneol treatment PMID: 20473716 Increased buffer concentration by addition of HEPES, MOPS, or TES to the media during differentiation increased independent of the type of buffer. This correlated with increased expression of claudin-5 PMID: 20967520 MUPP1 and claudin-5 colocalized in the incisures, and the COOH-terminal region of claudin-5 interacts with MUPP1 in a PSD-95/Disc Large/zona occludens (ZO)-1 (PDZ)-dependent manner in tight junctions PMID: 12403818 Induction of wild-type claudin-5 is sufficient to reconstitute the paracellular barrier against inulin (5 kDa), but not mannitol (182 Da), in leaky rat lung epithelial cells PMID: 15383327 Data show that adrenomedullin inhibits paracellular transport in a blood-brain barrier in vitro model through claudin-5 overexpression. PMID: 16763778 Claudin 5 is predominantly expressed in brain capillaries, and plays a key role in the appearance of barrier properties of brain capillary endothelial cells. PMID: 16998798 Immunogold electron microscopy demonstrated claudin-5 localized in the tight-junctional fused membranes of adjacent endothelial cells. PMID: 17899156

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.