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1000 results found for “cyclophilin”
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Name :
CCL28 HumanDescription:
Mucosae-Associated Epithelial Chemokine Human Recombinant (CCL28)
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
Product # :
CHM-353Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CCL28 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 108 amino acids and having a molecular mass of 12.3 kDa. The CCL28 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM PBS and 150mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.More Info
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Introduction
CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues. -
Synonyms
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CCL28 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL28 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CCL28 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SEAILPIASS CCTEVSHHIS RRLLERVNMC RIQRADGDCD LAAVILHVKR RRICVSPHNH TVKQWMKVQA AKKNGKGNVC HRKKHHGKRN SNRAHQGKHE TYGHKTPY.
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Background
What is the molecular weight/Mw of CCL28 HUMAN Protein?
CCL28 HUMAN Protein has a total Mw of 12.3kDa.
What is the source or expression system of CCL28 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL28 HUMAN Protein?
CCL28 HUMAN Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL28 HUMAN Protein?
Determined by its ability to chemoattract human lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of CCL28 HUMAN Protein?
SEAILPIASS CCTEVSHHIS RRLLERVNMC RIQRADGDCD LAAVILHVKR RRICVSPHNH TVKQWMKVQA AKKNGKGNVC HRKKHHGKRN SNRAHQGKHE TYGHKTPY.
What applications can CCL28 HUMAN Protein be used in?
CCL28 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL28 HUMAN Protein?
The endotoxin level is minimal, CCL28 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CCL28 MouseDescription:
Mucosae-Associated Epithelial Chemokine Mouse Recombinant (CCL28)
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
Product # :
CHM-369Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CCL28 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids and having a molecular mass of 12.6 kDa. The CCL28 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM Phosphate buffer pH-7.4 and 150mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract mouse lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.More Info
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Introduction
CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues. -
Synonyms
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CCL28 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL28 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CCL28 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SEAILPMASS CCTEVSHHVS GRLLERVSSC SIQRADGDCD LAAVILHVKR RRICISPHNR TLKQWMRASE VKKNGRENVC SGKKQPSRKD RKGHTTRKHR TRGTHRHEAS R.
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Background
What is the molecular weight/Mw of CCL28 MOUSE Protein?
CCL28 MOUSE Protein has a total Mw of 12.6kDa.
What is the source or expression system of CCL28 MOUSE Protein?
Escherichia Coli.
What is the Purity of CCL28 MOUSE Protein?
CCL28 MOUSE Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL28 MOUSE Protein?
Determined by its ability to chemoattract mouse lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of CCL28 MOUSE Protein?
SEAILPMASS CCTEVSHHVS GRLLERVSSC SIQRADGDCD LAAVILHVKR RRICISPHNR TLKQWMRASE VKKNGRENVC SGKKQPSRKD RKGHTTRKHR TRGTHRHEAS R.
What applications can CCL28 MOUSE Protein be used in?
CCL28 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL28 MOUSE Protein?
The endotoxin level is minimal, CCL28 MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CYB5A HumanDescription:
Cytochrome B5 Type A Human Recombinant
Cytochrome b5, Microsomal cytochrome b5 type A, MCB5, CYB5A, CYB5.
Product # :
PRO-910Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CYB5A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids (1-108 a.a) and having a molecular mass of 14.9kDa.CYB5A is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CYB5A protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Cytochrome b5 isoform 1 (CYB5A) is a member of the cytochrome b5 family. CYB5A is a membrane bound hemoprotein which functions as an electron carrier for several membrane bound oxygenases. Defects in the CYB5A gene are the cause of methemoglobinemia CYB5A-related (METHB-CYB5A), which is a form of methemoglobinemia (a hematologic disease characterized by the presence of excessive amounts of methemoglobin in blood cells, resulting in decreased oxygen carrying capacity of the blood, cyanosis and hypoxia).
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Synonyms
Cytochrome b5, Microsomal cytochrome b5 type A, MCB5, CYB5A, CYB5.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAEQSD EAVKYYTLEE IQKHNHSKST WLILHHKVYD LTKFLEEHPG GEEVLREQAG GDATENFEDV GHSTDAREMS KTFIIGELHP DDRPKLNKPP ETLITTIDSS SS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
pykF E.ColiDescription:
Pyruvate Kinase I E.Coli Recombinant
Pyruvate kinase I, PK-1, pykF, b1676, JW1666.
Product # :
PKA-028Price :
Quantity :
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Shipped with Ice Packs
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Description
pykF E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 494 amino acids (1-470 a.a) and having a molecular mass of 53.3kDa.pykF is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
pykF protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
pykF (pyruvate kinase I) is a member of the pyruvate kinase family. pykF is an enzyme involved in glycolysis. pykF catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to ADP, yielding one molecule of pyruvate and one molecule of ATP, a process which also requires a Magnesium ion. This is the final step in the glycolytic pathway, which produces pyruvate molecules, the ultimate product of aerobic glycolysis.
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Synonyms
Pyruvate kinase I, PK-1, pykF, b1676, JW1666.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMKKTKI VCTIGPKTES EEMLAKMLDA GMNVMRLNFS HGDYAEHGQR IQNLRNVMSK TGKTAAILLD TKGPEIRTMK LEGGNDVSLK AGQTFTFTTD KSVIGNSEMV AVTYEGFTTD LSVGNTVLVD DGLIGMEVTA IEGNKVICKV LNNGDLGENK GVNLPGVSIA LPALAEKDKQ DLIFGCEQGV DFVAASFIRK RSDVIEIREH LKAHGGENIH IISKIENQEG LNNFDEILEA SDGIMVARGD LGVEIPVEEV IFAQKMMIEK CIRARKVVIT ATQMLDSMIK NPRPTRAEAG DVANAILDGT DAVMLSGESA KGKYPLEAVS IMATICERTD RVMNSRLEFN NDNRKLRITE AVCRGAVETA EKLDAPLIVV ATQGGKSARA VRKYFPDATI LALTTNEKTA HQLVLSKGVV PQLVKEITST DDFYRLGKEL ALQSGLAHKG DVVVMVSGAL VPSGTTNTAS VHVL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ERLIN2 HumanDescription:
ER Lipid Raft Associated 2 Protein Human Recombinant
Erlin-2, Endoplasmic reticulum lipid raft-associated protein 2, Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 2, SPFH domain-containing protein 2,ERLIN2, C8orf2, SPFH2, UNQ2441, PRO5003, PRO9924, NET32, SPG18.
Product # :
PRO-1266Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ERLIN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 338 amino acids (25-339 a.a) and having a molecular mass of 37.8 kDa.ERLIN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ERLIN2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2M Urea and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ER Lipid Raft Associated 2 (ERLIN2) is a domain-containing protein which is a member of the band 7/mec-2 family. ERLIN2 is a ubiquitously expressed 339 amino acid protein.ERLIN2 which is localized to the lipid raft-like domains in the membrane of the endoplasmic reticulum (ER), plays a key role in the ER-associated degradation (ERAD) pathway that eliminates metabolically regulated and abnormal proteins from the ER.
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Synonyms
Erlin-2, Endoplasmic reticulum lipid raft-associated protein 2, Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 2, SPFH domain-containing protein 2,ERLIN2, C8orf2, SPFH2, UNQ2441, PRO5003, PRO9924, NET32, SPG18.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSKIEEGHI GVYYRGGALL TSTSGPGFHL MLPFITSYKS VQTTLQTDEV KNVPCGTSGG VMIYFDRIEV VNFLVPNAVY DIVKNYTADY DKALIFNKIH HELNQFCSVH TLQEVYIELF DQIDENLKLA LQQDLTSMAP GLVIQAVRVT KPNIPEAIRR NYELMESEKT KLLIAAQKQK VVEKEAETER KKALIEAEKV AQVAEITYGQ KVMEKETEKK ISEIEDAAFL AREKAKADAE CYTAMKIAEA NKLKLTPEYL QLMKYKAIAS NSKIYFGKDI PNMFMDSAGS VSKQFEGLAD KLSFGLEDEP LETATKEN.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ARL6 HumanDescription:
ADP-Ribosylation Factor-Like 6 Human Recombinant
ADP-ribosylation factor-like 6, Bardet-Biedl syndrome 3 protein, BBS3, RP55, MGC32934.
Product # :
PRO-232Price :
Quantity :
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Shipped with Ice Packs
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Description
ARL6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (1-186a.a) and having a molecular mass of 23.2kDa.ARL6 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARL6 protein solution (0.5mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.2M NaCl and 5mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ARL6 is a member of the ARF family of GTP-binding proteins. ARL6 has a vital part in modulating membrane trafficking and cytoskeletal functions. Mutation in ARL6 is the source of Bardet-Biedl syndrome (BBS3) which is a pleiotropic genetic disorder that causes obesity, photoreceptor degeneration, polydactyly, hypogenitalism, renal abnor-malities and developmental delay.
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Synonyms
ADP-ribosylation factor-like 6, Bardet-Biedl syndrome 3 protein, BBS3, RP55, MGC32934.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGLLDRLSVL LGLKKKEVHV LCLGLDNSGK TTIINKLKPS NAQSQNILPT IGFSIEKFKS SSLSFTVFDM SGQGRYRNLW EHYYKEGQAI IFVIDSSDRL RMVVAKEELD TLLNHPDIKH RRIPILFFAN KMDLRDAVTS VKVSQLLCLE NIKDKPWHIC ASDAIKGEGL QEGVDWLQDQ IQTVKT.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SAR1A HumanDescription:
GTP-Binding Protein SAR1A Human Recombinant
GTP-binding protein SAR1a, COPII-associated small GTPase, SAR1A, SAR1, SARA, SARA1.
Product # :
PRO-709Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SAR1A Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 218 amino acids (1- 198 a.a.) and having a molecular mass of 24.5kDa.The SAR1A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SAR1A solution contains 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
SAR1A is a member of the small GTPase superfamily. SAR1A is a vital component of COPII vesicle coats involved in export of cargo from the ER (Endoplasmic Reticulum). The GTPase activity of SAR1A serves as a molecular switch to control protein-protein and protein-lipid interactions which dictate vesicle budding from the ER. SAR1A, while GDP-bound interacts with the membrane-bound exchange factor Sec12 and trades its bound GDP for GTP. SAR1A is also involved in the transport from the ER to the Golgi apparatus. SAR1A is required to maintain SEC16A localization at distinct locations on the ER membrane possibly by preventing its dissociation. SAR1A-GTP-dependent compilation of SEC16A on the ER membrane creates a structured scaffold defining endoplasmic reticulum exit sites.
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Synonyms
GTP-binding protein SAR1a, COPII-associated small GTPase, SAR1A, SAR1, SARA, SARA1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSFIFEWIYN GFSSVLQFLG LYKKSGKLVF LGLDNAGKTT LLHMLKDDRL GQHVPTLHPT SEELTIAGMT FTTFDLGGHE QARRVWKNYL PAINGIVFLV DCADHSRLVE SKVELNALMT DETISNVPIL ILGNKIDRTD AISEEKLREI FGLYGQTTGK GNVTLKELNA RPMEVFMCSV LKRQGYGEGF RWLSQYID.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MORC3 HumanDescription:
MORC Family CW-Type Zinc Finger 3 Human Recombinant
MORC family CW-type zinc finger protein 3, Nuclear matrix protein 2, Zinc finger CW-type coiled-coil domain protein 3, MORC3, KIAA0136, NXP2, ZCWCC3.
Product # :
PRO-2674Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human MORC Family CW-Type Zinc Finger 3 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 122kDa. MORC3 is expressed with a 10xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
MORC3 is supplied in 20mM Sodium phosphate, pH 7.6, 500mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
MORC Family CW-Type Zinc Finger 3 (MORC3) localizes to the nuclear matrix. MORC3 takes part in the regulation of the tumor suppressor protein p53. MORC3may indicate on dermatomyositis (DM) as autoantibodies against this protein have been found in patients.
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Synonyms
MORC family CW-type zinc finger protein 3, Nuclear matrix protein 2, Zinc finger CW-type coiled-coil domain protein 3, MORC3, KIAA0136, NXP2, ZCWCC3.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG-type human auto-antibodies.2. immunodot test with positive/negative samples.
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Applications
Western blot with patient sample.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Prealbumin HumanDescription:
Transthyretin Human
TTHY, TTR, ATTR, TBPA, Transthyretin, Prealbumin, PALB, HsT2651TTHY, TTR, ATTR, TBPA, Transthyretin, Prealbumin, PALB, HsT2651.
Product # :
PRO-2740Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Transthyretin dimer protein produced in Human plasma having a molecular mass of 30kD. Under certain conditions it may be shown as a monomer (15kD) or a tetramer (60kD).
Source
Human serum.
Formulation
The protein was lyophilized (0.2 µm filtered) from 20mM NH4HCO3.
Purity
Greater than 96.0%.
More Info
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Introduction
Prealbumin is a thyroid hormone-binding protein that transports thyroxine from the bloodstream to the brain. Prealbumin is a carrier protein which transports thyroid hormones in the plasma and cerebrospinal fluid, and also transports retinol (vitamin A) in the plasma. Transthyretin consists of a tetramer of identical subunits and is dominantly produced in the liver. Mutations in Prealbumin are related to amyloid deposition, affecting predominantly peripheral nerve and/or the heart. The diseases caused by mutations include amyloidotic polyneuropathy, euthyroid hyperthyroxinaemia, amyloidotic vitreous opacities, cardiomyopathy, oculoleptomeningeal amyloidosis, meningocerebrovascular amyloidosis, and carpal tunnel syndrome. Prealbumin is an indicator of protein-energy malnutrition since it has a circulating half life of 2 days and reacts swiftly to changes in nutritional status.
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Synonyms
TTHY, TTR, ATTR, TBPA, Transthyretin, Prealbumin, PALB, HsT2651TTHY, TTR, ATTR, TBPA, Transthyretin, Prealbumin, PALB, HsT2651.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Prealbumin Human although stable at room temperature for 3 weeks, should be stored between 2-8°C.
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Solubility
It is recommended to reconstitute the lyophilized Prealbumin Human in phosphate buffer pH > 7 containing 0.15M NaCl.
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Human Virus Test
Starting material donor has been tested and certified negative for antibodies to HIV-1, HIV-2, HCV, HBSAG, Parvovirus B19, Syphilis and HIV/HBV/HCV (PCR).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CXCL16 HumanDescription:
CXCL16 Human Recombinant
Chemokine (C-X-C Motif) Ligand 16, Scavenger Receptor For Phosphatidylserine And Oxidized Low Density Lipoprotein, Transmembrane Chemokine CXCL16, Small-Inducible Cytokine B16, CXC Chemokine Ligand 16, SR-PSOX, SRPSOX, C-X-C Motif Chemokine 16, CXCLG16, SCYB16, CXCL16.
Product # :
CHM-029Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CXCL16 Human Recombinant (30-118 a.a.) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 89 amino acids and having a molecular mass of 10kDa.The CXCL16 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CXCL16 protein was lyophilized from a 0.2µm filtered solution in PBS.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured by its ability to chemoattract mouse CXCR6-transfected mouse BaF3 cells, is less than 12ng/ml.More Info
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Introduction
CXC chemokine ligand 16 (CXCL16) is a type I membrane protein, which contains a non-ELR motif-containing CXC chemokine domain in its extracellular region. Human and Mouse CXCL16 share a 70% a.a. sequence similarity within their chemokine domains and 49% overall a.a. sequence identity. Functional CXCL16 can be dropped from the cell surface as an approximately 35kDa soluble protein. CXCR6 is the functional receptor for CXCL16. CXCL16 functions as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), proposing that CXCL16 may be involved in pathophysiology such as atherogenesis. In addition, CXCL16 induces a strong chemotactic response and calcium mobilization. CXCL16 binds to CXCR6/Bonzo.
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Synonyms
Chemokine (C-X-C Motif) Ligand 16, Scavenger Receptor For Phosphatidylserine And Oxidized Low Density Lipoprotein, Transmembrane Chemokine CXCL16, Small-Inducible Cytokine B16, CXC Chemokine Ligand 16, SR-PSOX, SRPSOX, C-X-C Motif Chemokine 16, CXCLG16, SCYB16, CXCL16.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CXCL16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL16 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CXCL16 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
NEGSVTGSCY CGKRISSDSP PSVQFMNRLR KHLRAYHRCL YYTRFQLLSW SVCGGNKDPW VQELMSCLDL KECGHAYSGI VAHQKHLLP.
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Background
What is the molecular weight/Mw of CXCL16 HUMAN Protein?
CXCL16 HUMAN Protein has a total Mw of 10kDa.
What is the source or expression system of CXCL16 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL16 HUMAN Protein?
CXCL16 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL16 HUMAN Protein?
The ED50, as measured by its ability to chemoattract mouse CXCR6-transfected mouse BaF3 cells, is less than 12ng/ml.
What is the amino acid sequence of CXCL16 HUMAN Protein?
NEGSVTGSCY CGKRISSDSP PSVQFMNRLR KHLRAYHRCL YYTRFQLLSW SVCGGNKDPW VQELMSCLDL KECGHAYSGI VAHQKHLLP.
What applications can CXCL16 HUMAN Protein be used in?
CXCL16 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL16 HUMAN Protein?
The endotoxin level is minimal, CXCL16 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
AITRL HumanDescription:
AITRL Human Recombinant
Osteostat, TNFSF18, Activation-induced TNFR member Ligand, GITRL,TL6, AITRL, Glucocorticoid-induced TNF-related ligand, hGITRL, Tumor necrosis factor ligand superfamily member 18, MGC138237.
Product # :
CYT-076Price :
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Shipped with Ice Packs
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- sds-page
Description
AITRL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 129 amino acids (72-199) and having a molecular mass of 14.6 kDa.AITRL is purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The AITRL solution (0.5mg/ml) contains 10mM sodium citrate (pH 3.5), 1mMDTT and 10% glycerol
Purity
Greater than 90% as determined by SDS-PAGE.
sds-page
More Info
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Synonyms
Osteostat, TNFSF18, Activation-induced TNFR member Ligand, GITRL,TL6, AITRL, Glucocorticoid-induced TNF-related ligand, hGITRL, Tumor necrosis factor ligand superfamily member 18, MGC138237.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MQLETAKEPC MAKFGPLPSK WQMASSEPPC VNKVSDWKLE ILQNGLYLIY GQVAPNANYN DVAPFEVRLY KNKDMIQTLT NKSKIQNVGG TYELHVGDTI DLIFNSEHQV LKNNTYWGII LLANPQFIS
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Background
AITRL Human Recombinant: Unraveling its Significance in Immune Modulation and Therapeutic Implications
1. Abstract
This research paper provides a comprehensive examination of AITRL Human Recombinant, an essential protein involved in immune modulation. By exploring its structure, signaling mechanisms, biological functions, and implications in disease pathology, we shed light on the potential therapeutic applications of AITRL in immune-related disorders.
2. Introduction
AITRL, also known as TNFSF18, is a receptor protein belonging to the tumor necrosis factor superfamily. It plays a crucial role in immune regulation and has emerged as an intriguing target for therapeutic interventions in various immune-mediated conditions.
3. Structure and Signaling of AITRL
AITRL is a transmembrane protein with a conserved TNF domain. It interacts with its receptor, AITR (TNFRSF18), leading to downstream signaling events that modulate immune cell function. The binding of AITRL to AITR promotes immune cell activation and cytokine production.
4. Biological Functions of AITRL
AITRL is involved in the regulation of immune responses by influencing T-cell activation, proliferation, and differentiation. It can stimulate effector T-cell responses while also promoting the development and function of regulatory T cells, thus maintaining immune homeostasis.
5. AITRL in Disease Pathology
Dysregulation of AITRL signaling has been implicated in various immune-related disorders, including autoimmune diseases, allergic reactions, and cancer. AITRL's involvement in disease pathology highlights its significance as a potential therapeutic target.
6. Therapeutic Potential of AITRL
The unique role of AITRL in immune modulation presents opportunities for therapeutic interventions. Modulating AITRL signaling holds promise for manipulating immune responses in the context of autoimmune diseases, allergic disorders, and cancer immunotherapy.
7. Conclusion and Future Perspectives
While our understanding of AITRL and its functions has advanced significantly, further research is needed to unravel its complex signaling pathways and therapeutic potential fully. Continued investigations into AITRL biology will pave the way for the development of targeted therapies for immune-related disorders.
What is the molecular weight/Mw of AITRL Protein?
AITRL Protein has a total Mw of 15.6kDa.
What is the source or expression system of AITRL Protein?
Escherichia Coli.
What is the Purity of AITRL Protein?
AITRL Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of AITRL Protein?
The biological functionality of AITRL Protein will be determined in the future.
What is the amino acid sequence of AITRL Protein?
MQLETAKEPC MAKFGPLPSK WQMASSEPPC VNKVSDWKLE ILQNGLYLIY GQVAPNANYN DVAPFEVRLY KNKDMIQTLT NKSKIQNVGG TYELHVGDTI DLIFNSEHQV LKNNTYWGII LIANPQEISL EHHHHHH.
What applications can AITRL Protein be used in?
AITRL Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for AITRL Protein?
The endotoxin level is minimal, AITRL Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TFPI HumanDescription:
Tissue Factor Pathway Inhibitor Human Recombinant
Tissue Factor Pathway Inhibitor (Lipoprotein-Associated Coagulation Inhibitor), Extrinsic Pathway Inhibitor, Tissue Factor Pathway Inhibitor, anti-convertin, TFPI1, EPI, LACI, TFI.
Product # :
PRO-1702Price :
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Description
TFPI Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 299 amino acids (29-304) and having a molecular mass of 34.3kDa.TFPI is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TFPI solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
TFPI is a protease inhibitor which controls the tissue factor (TF)-dependent pathway of blood coagulation. The coagulation process starts with the creation of a factor VIIa-TF complex, that proteolytically triggers additional proteases (factors IX and X) and eventually results in a fibrin clot. TFPI inhibits the activated factor X and VIIa-TF proteases in an autoregulatory loop. TFPI is glycosylated and predominantly located in the vascular endothelium and plasma in both free forms and complexed with plasma lipoproteins. A number of alternatively spliced transcript variants of this gene have are known, however the full-length nature of several of these variants were not yet established.
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Synonyms
Tissue Factor Pathway Inhibitor (Lipoprotein-Associated Coagulation Inhibitor), Extrinsic Pathway Inhibitor, Tissue Factor Pathway Inhibitor, anti-convertin, TFPI1, EPI, LACI, TFI.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDSEEDEE HTIITDTELP PLKLMHSFCA FKADDGPCKA IMKRFFFNIF TRQCEEFIYG GCEGNQNRFE SLEECKKMCT RDNANRIIKT TLQQEKPDFC FLEEDPGICR GYITRYFYNN QTKQCERFKY GGCLGNMNNF ETLEECKNIC EDGPNGFQVD NYGTQLNAVN NSLTPQSTKV PSLFEFHGPS WCLTPADRGL CRANENRFYY NSVIGKCRPF KYSGCGGNEN NFTSKQECLR ACKKGFIQRI SKGGLIKTKR KRKKQRVKIA YEEIFVKNM.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GPC3 HumanDescription:
Glypican-3 Human Recombinant
Glypican 3, Intestinal Protein OCI-5, Glypican Proteoglycan 3, GTR2-2, MXR7, Heparan Sulphate Proteoglycan, Secreted Glypican-3, Glypican-3, OCI-5, SGBS1, DGSX, SGBS, SDYS, OCI5, SGB, GPC3.
Product # :
PRO-2423Price :
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Description
GPC3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 544 amino acids (25-559a.a.) and having a molecular mass of 61.8kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). GPC3 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
GPC3 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Glypican-3 (GPC3) belongs to the glypican family, and is highly expressed in the lung, liver, and the kidney. In some tissues, GPC3 functionss as a tumor suppressor gene and an oncofetal protein. The Glypican-3 protein is currently considered as a tumor marker and potential target for immunotherapy. Glypican-3 binds to and inhibits the dipeptidyl peptidase activity of CD26, and it can also induce apoptosis in certain cell types. Deletion mutations in the GPC3 gene are linked with Simpson-Golabi-Behmel syndrome, aka Simpson dysmorphia syndrome.
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Synonyms
Glypican 3, Intestinal Protein OCI-5, Glypican Proteoglycan 3, GTR2-2, MXR7, Heparan Sulphate Proteoglycan, Secreted Glypican-3, Glypican-3, OCI-5, SGBS1, DGSX, SGBS, SDYS, OCI5, SGB, GPC3.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPQPPPPPP DATCHQVRSF FQRLQPGLKW VPETPVPGSD LQVCLPKGPT CCSRKMEEKY QLTARLNMEQ LLQSASMELK FLIIQNAAVF QEAFEIVVRH AKNYTNAMFK NNYPSLTPQA FEFVGEFFTD VSLYILGSDI NVDDMVNELF DSLFPVIYTQ LMNPGLPDSA LDINECLRGA RRDLKVFGNF PKLIMTQVSK SLQVTRIFLQ ALNLGIEVIN TTDHLKFSKD CGRMLTRMWY CSYCQGLMMV KPCGGYCNVV MQGCMAGVVE IDKYWREYIL SLEELVNGMY RIYDMENVLL GLFSTIHDSI QYVQKNAGKL TTTIGKLCAH SQQRQYRSAY YPEDLFIDKK VLKVAHVEHE ETLSSRRREL IQKLKSFISF YSALPGYICS HSPVAENDTL CWNGQELVER YSQKAARNGM KNQFNLHELK MKGPEPVVSQ IIDKLKHINQ LLRTMSMPKG RVLDKNLDEE GFESGDCGDD EDECIGGSGD GMIKVKNQLR FLAELAYDLD VDDAPGNSQQ ATPKDNEIST FHNLGNVHHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
VEGF HumanDescription:
Vascular Endothelial Growth Factor Human Recombinant
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Product # :
CYT-241Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Vascular Endothelial Growth Factor Human Recombinant produced in E.Coli is a double, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 38.2kDa.The VEGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The VEGF protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by the dose-dependent stimulation of the proliferation of human umbilical vein endothelial cells (HUVEC) using a concentration range of 3.7-5.6 ng/ml, corresponding to a Specific Activity of 178,570-270,270IU/mg.More Info
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Introduction
Vascular endothelial growth factor (VEGF) is an important signaling protein involved in vessel formation As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ). VEGF mediates increased vascular permeability, induces vasculogenesis and endothelial cell production, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor. VEGF is located in normal cartilage though only osteoarthritic cartilage expresses the VEGF receptors, NP1, VEGFR1 and VEGFR2. The VEGF level in the culture media from OA chondrocytes was more than 3 folds higher than in media from normal chondrocytes
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Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized VEGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized VEGF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
APMAEGGGQN HHEVVKFMDV YQRSYCHPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TEESNITMQI MRIKPHQGQH IGEMSFLQHN KCECRPKKDR ARQENPCGPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR
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Protein content
VEGF protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.2875 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of VEGF as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SERTAD1 HumanDescription:
SERTA Domain Containing 1 Human Recombinant
SERTA domain-containing protein 1, CDK4-binding protein p34SEI1, SEI-1, Transcriptional regulator interacting with the PHD-bromodomain 1, TRIP-Br1, SERTAD1, SEI1.
Product # :
PRO-1157Price :
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Description
SERTAD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 260 amino acids (1-236 a.a) and having a molecular mass of 27.3kDa (Molecular weight on SDS-PAGE will appear higher).SERTAD1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SERTAD1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
SERTA domain-containing protein (SERTAD1) functions with E2F-responsive promoters to integrate signals provided by PHD- and/or bromodomain-containing transcription factors. SERTAD1 stimulates E2F-1/DP-1 transcriptional activity. SERTAD1 reduces the activity of cyclin D1/CDK4 resistant to the inhibitory effects of p16(INK4a). In addition, SERTAD1 interacts with the PHD-bromodomain of TIF1, TRIM28/TIF1B and p300/CBP. Furthermore, SERTAD1 binds to DP1 and interacts with CDK4.
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Synonyms
SERTA domain-containing protein 1, CDK4-binding protein p34SEI1, SEI-1, Transcriptional regulator interacting with the PHD-bromodomain 1, TRIP-Br1, SERTAD1, SEI1.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMLSKGL KRKREEEEEK EPLAVDSWWL DPGHTAVAQA PPAVASSSLF DLSVLKLHHS LQQSEPDLRH LVLVVNTLRR IQASMAPAAA LPPVPSPPAA PSVADNLLAS SDAALSASMA SLLEDLSHIE GLSQAPQPLA DEGPPGRSIG GAAPSLGALD LLGPATGCLL DDGLEGLFED IDTSMYDNEL WAPASEGLKP GPEDGPGKEE APELDEAELD YLMDVLVGTQ ALERPPGPGR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CXCL1 Human, HisDescription:
GRO-Alpha/MGSA Human Recombinant (CXCL1), His Tag
Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha(1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.
Product # :
CHM-242Price :
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Description
CXCL1 Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 94 amino acids (35-107) and having a molecular mass of 10.1 kDa. The CXCL1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CXCL1 in 20mM Tris-HCL pH-8 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Chemokine (C-X-C motif) ligand 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-?). It is secreted by human melanoma cells, has mitogenic properties and is implicated in melanoma pathogenesis. CXCL1 is expressed by macrophages, neutrophils and epithelial cells, and has neutrophil chemoattractant activity. CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis. This chemokine elicits its effects by signaling through the chemokine receptor CXCR2. The gene for CXCL1 is located on human chromosome 4 amongst genes for other CXC chemokines.
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Synonyms
Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha(1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Liquid CXCL1 although stable at 10°C for 1 week, should be stored below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASVATELRC QCLQTLQGIH PKNIQSVNVK SPGPHCAQTE VIATLKNGRK ACLNPASPIV KKIIEKMLNS DKSN.
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Background
What is the molecular weight/Mw of CXCL1 HUMAN, HIS Protein?
CXCL1 HUMAN, HIS Protein has a total Mw of 10.1kDa.
What is the source or expression system of CXCL1 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CXCL1 HUMAN, HIS Protein?
CXCL1 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL1 HUMAN, HIS Protein?
The biological functionality of CXCL1 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CXCL1 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MASVATELRC QCLQTLQGIH PKNIQSVNVK SPGPHCAQTE VIATLKNGRK ACLNPASPIV KKIIEKMLNS DKSN.
What applications can CXCL1 HUMAN, HIS Protein be used in?
CXCL1 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL1 HUMAN, HIS Protein?
The endotoxin level is minimal, CXCL1 HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
iL22RA (Y51A) Mouse, PEGDescription:
Interleukin-22 Receptor Antagonist (Y51A), PEG Mouse Recombinant
Product # :
CYT-1248Price :
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Shipped at Room temp
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Description
Interleukin 22 Y51A mutan Mouse Recombinant is a single non-glycosilated polypeptide chain containing 147 amino acids and additional Ala at N-terminus. The iL22RA is bound to 20 kDa PEG molecule at N-terminus, resulting in 36.0 kDa. The Mouse iL22RA (Y51A) Pegylated runs as a 50 kDa due to enlarged hydrodymanic volume. iL22RA Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Mouse iL22RA (Y51A) was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Pegylated Mouse iL22RA inhibits mouse IL-22 induced STAT3 phosphorylation in HepG cells. Its inhibitory acrtivity in vitro is ~ 10-20% compared to the non-pegylated mIL22 (Y51A) mutant.
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized iL22RA (Y51A) Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2mM and filter sterilization iL22RA mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized iL22RA (Y51A) Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Background
IL-22 is a part of the IL-10 family of regulatory cytokines and produced by several populations of immune cells at a site of inflammation. Members of this family share partial homology in their amino acid sequences, but varies in their biological functions. IL-22 takes effect on non-hematopoietic cells. IL-22 takes part in wound healing and in protection against microbs. Produced by T lymphocytes, IL-22 inhibits IL-4 production by Th2 cells, and induces acute phase reactants in the pancreas and liver.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.18 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
KLRB1 Human, Sf9Description:
Killer Cell Lectin-Like Receptor Subfamily B, Member 1 Human Recombinant, Sf9
Killer Cell Lectin Like Receptor B1, Natural Killer Cell Surface Protein P1A, Killer Cell Lectin-Like Receptor Subfamily B, Member 1, C-Type Lectin Domain Family 5 Member B, HNKR-P1A, NKR-P1A, CLEC5B, NKRP1A, Killer Cell Lectin-Like Receptor Subfamily B Member 1, CD161 Antigen, NKR-P1, CD161, NKR.
Product # :
PRO-2488Price :
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Description
KLRB1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 401 amino acids (67-225a.a.) and having a molecular mass of 45.7kDa. KLRB1 is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
KLRB1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
KLRB1 has an inhibitory role on natural killer (NK) cells cytotoxicity which are lymphocytes who facilitate cytotoxicity and secrete cytokines subsequent to immune stimulation. Some genes of the C-type lectin superfamily, like the rodent NKRP1 family of glycoproteins, are expressed by NK cells and take part in NK cell function regulation. KLRB1 holds an extracellular domain with a few characteristic motifs of C-type lectins, a transmembrane domain, and a cytoplasmic domain. Due to its external C terminus KLRB1 is considered to be a type II membrane protein.
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Synonyms
Killer Cell Lectin Like Receptor B1, Natural Killer Cell Surface Protein P1A, Killer Cell Lectin-Like Receptor Subfamily B, Member 1, C-Type Lectin Domain Family 5 Member B, HNKR-P1A, NKR-P1A, CLEC5B, NKRP1A, Killer Cell Lectin-Like Receptor Subfamily B Member 1, CD161 Antigen, NKR-P1, CD161, NKR.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPQKSSIEK CSVDIQQSRN KTTERPGLLN CPIYWQQLRE KCLLFSHTVN PWNNSLADCS TKESSLLLIR DKDELIHTQN LIRDKAILFW IGLNFSLSEK NWKWINGSFL NSNDLEIRGD AKENSCISIS QTSVYSEYCS TEIRWICQKE LTPVRNKVYP DSLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PF4 BovineDescription:
Platelet Factor-4 (CXCL4) Bovine Recombinant
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
Product # :
CHM-039Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Platelet Factor-4 (CXCL4) Bovine Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 88 amino acid and having a molecular mass of approximately 9.5kDa.PF4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in 20 mM PB and 500mM NaCl, pH 7.0.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity determined by a chemotaxis bioassay using human neutrophils is 10-100ng/ml.
More Info
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Introduction
Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets.PF4’s major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemokine family. Furthermore, it is used as an inhibitor in the angiogenesis during tumor therapy.
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Synonyms
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CXCL4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Platelet Factor-4 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Platelet Factor-4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
ESSFPATFVP LPADSEGGED EDLQCVCLKT TSGINPRHIS SLEVIGAGTH CPSPQLLATK KTGRKICLDQ QRPLYKKILK KLLDGDES.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CCL6 RatDescription:
C-10 Rat Recombinant (CCL6)
Small inducible cytokine A6, CCL6, C10 protein, c10, MRP-1, Scya6, chemokine (C-C motif) ligand 6.
Product # :
CHM-268Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
C-10 Rat Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 94 amino acids and having a total molecular mass of 10.4kDa. C-10 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 1×PBS, pH 7.4.
Purity
Greater than 95.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human CCR1 transfected BaF3 mouse proB cells using a concentration range of 0.05-0.25 ug/ml.More Info
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Introduction
Chemokine (C-C motif) ligand 6 (CCL6) is a small cytokine belonging to the CC chemokine family that has only been identified in rodents.
In mice, CCL6 is expressed in cells from neutrophil and macrophage lineages, and can be greatly induced under conditions suitable for myeloid cell differentiation. It is highly expressed in bone marrow cultures that have been stimulated with the cytokine GM-CSF. Some low levels of gene expression also occur in certain cell lines of myeloid origin (e.g. the immature myeloid cell lines DA3 and 32D cl3, and the macrophage cell line P388D) that can also be greatly induced in culture with GM-CSF. However, in activated T cell lines, expression of CCL6 is greatly reduced. CCL6 can also be induced in the mouse lung by the cytokine interleukin 13. Mouse CCL6 is located on chromosome 11. The cell surface receptor for CCL6 is believed to be the chemokine receptor CCR1. -
Synonyms
Small inducible cytokine A6, CCL6, C10 protein, c10, MRP-1, Scya6, chemokine (C-C motif) ligand 6.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized C-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution C-10 should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized C-10 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
GLIQDTVKED RPFNPTIIHQ GFQDSSDCCF SYASQIPCSR FIYYFPTSGG CTKPGIIFVT RKRKRVCANP SDQRVQTCIS TLKLGPRSGN SAIA.
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Background
What is the molecular weight/Mw of CCL6 RAT Protein?
CCL6 RAT Protein has a total Mw of 10.4kDa.
What is the source or expression system of CCL6 RAT Protein?
Escherichia Coli.
What is the Purity of CCL6 RAT Protein?
CCL6 RAT Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL6 RAT Protein?
Determined by its ability to chemoattract human CCR1 transfected BaF3 mouse proB cells using a concentration range of 0.05-0.25 ug/ml.
What is the amino acid sequence of CCL6 RAT Protein?
GLIQDTVKED RPFNPTIIHQ GFQDSSDCCF SYASQIPCSR FIYYFPTSGG CTKPGIIFVT RKRKRVCANP SDQRVQTCIS TLKLGPRSGN SAIA.
What applications can CCL6 RAT Protein be used in?
CCL6 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL6 RAT Protein?
The endotoxin level is minimal, CCL6 RAT Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IP 10 MouseDescription:
IP-10 Mouse Recombinant (CXCL10)
Small inducible cytokine B10, CXCL10, 10 kDa, Gamma-IP10, IP-10, chemokine (C-X-C motif) ligand 10, C7, IFI10, INP10, crg-2, mob-1, SCYB10, gIP-10.
Product # :
CHM-336Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- sds-page
Description
IP-10 Mouse Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 77 amino acids and having a molecular mass of 8701 Dalton. The IP-10 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IP-10 was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract hCXCR3/HEK293 cells using a concentration range of 100.0-500.0 ng/ml.sds-page
More Info
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Introduction
Chemokine (C-X-C motif) ligand 10 (CXCL10) is a small cytokine belonging to the CXC chemokine family. CXCL10 is secreted by several cell types. These cell types include monocytes, endothelial cells and fibroblasts. CXCL10 has been attributed to several roles, such as chemoattraction for monocytes and T cells, promotion of T cell adhesion to endothelial cells, antitumor activity, and inhibition of bone marrow colony formation and angiogenesis. The gene for CXCL10 is located on human chromosome 4 in a cluster among several other CXC chemokines. This chemokine elicits its effects by binding to the cell surface chemokine receptor CXCR3. The three-dimensional crystal structure of this chemokine has been determined under 3 different conditions to a resolution of up to 1.92A.
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Synonyms
Small inducible cytokine B10, CXCL10, 10 kDa, Gamma-IP10, IP-10, chemokine (C-X-C motif) ligand 10, C7, IFI10, INP10, crg-2, mob-1, SCYB10, gIP-10.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IP-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL10 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized IP-10 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
IPLARTVRCN CIHIDDGPVR MRAIGKLEII PASLSCPRVE IIATMKKNDE QRCLNPESKT IKNLMKAFSQ KRSKRAP.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.02 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IP-10 as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ANGPTL7 HumanDescription:
Angiopoietin-like Protein 7 Human Recombinant
angiopoietin like 7, AngX, CDT6, dJ647M16.1, Angiopoietin-like factor; Angiopoietin-like Protein 7, ANGPTL7, angiopoietinrelated protein 7, Cornea-derived transcript 6 protein
Product # :
CYT-1208Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ANGPTL7 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (27-346a.a) containing 553amino acids and having a molecular mass of 63.2kDa.ANGPTL7 is fused to a 233 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
ANGPTL7 protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Angiopoietin-related protein 7 (ANGPTL7), belongs to the angiopoietin-like family of molecules. ANGPTL7 is expressed in the corneal stroma, trabecular meshwork, and sclera. ANGPTL7 production is up-regulated in trabecular meshwork cells by glucocorticoids and TGF-Beta and in cartilage by TNF-alpha.
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Synonyms
angiopoietin like 7, AngX, CDT6, dJ647M16.1, Angiopoietin-like factor; Angiopoietin-like Protein 7, ANGPTL7, angiopoietinrelated protein 7, Cornea-derived transcript 6 protein
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
QKLSKHKTPA QPQLKAANCC EEVKELKAQV ANLSSLLSEL NKKQERDWVS VVMQVMELES NSKRMESRLT DAESKYSEMN NQIDIMQLQA AQTVTQTSAD AIYDCSSLYQ KNYRISGVYK LPPDDFLGSP ELEVFCDMET SGGGWTIIQR RKSGLVSFYR DWKQYKQGFG SIRGDFWLGN EHIHRLSRQP TRLRVEMEDW EGNLRYAEYS HFVLGNELNS YRLFLGNYTG NVGNDALQYH NNTAFSTKDK DNDNCLDKCA QLRKGGYWYN CCTDSNLNGV YYRLGEHNKH LDGITWYGWH GSTYSLKRVE MKIRPEDFKP LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK
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Background
Angiopoietin-like Protein 7 Human Recombinant: An Emerging Player in Metabolic Regulation and Therapeutic Potential
Abstract:
Angiopoietin-like protein 7 (ANGPTL7) is a multifunctional protein that has recently gained attention for its potential role in metabolic regulation and as a therapeutic target for metabolic disorders. ANGPTL7 is involved in the modulation of lipid metabolism, adipogenesis, and insulin signaling. The availability of human recombinant ANGPTL7 protein has provided researchers with a valuable tool to unravel its biological functions and explore its therapeutic applications. This review provides an overview of the current knowledge on ANGPTL7 and discusses its potential as a therapeutic intervention in metabolic disorders.
Introduction:
Metabolic disorders, including obesity and type 2 diabetes, pose significant health challenges worldwide. ANGPTL7, a member of the angiopoietin-like protein family, has recently emerged as a potential regulator of metabolic processes. ANGPTL7 affects lipid metabolism, adipose tissue biology, and insulin signaling pathways, making it an intriguing target for therapeutic interventions in metabolic disorders.
Role of ANGPTL7 in Metabolic Regulation:
ANGPTL7 plays a multifaceted role in metabolic regulation. It influences lipid metabolism by regulating lipoprotein lipase (LPL) activity and lipid uptake in adipose tissue and skeletal muscle. ANGPTL7 also affects adipocyte biology and adipogenesis, potentially contributing to the development of obesity and related metabolic complications. Furthermore, ANGPTL7 modulates insulin signaling and glucose metabolism, suggesting its involvement in insulin resistance and diabetes pathogenesis.
Mechanisms of ANGPTL7 Action:
ANGPTL7 exerts its effects through various mechanisms. It interacts with extracellular matrix components, influencing cell adhesion and migration. ANGPTL7 also regulates angiogenesis and vascular remodeling, potentially linking it to metabolic regulation and tissue homeostasis.
Therapeutic Potential of ANGPTL7 Human Recombinant Protein:
The availability of ANGPTL7 human recombinant protein offers new avenues for therapeutic interventions in metabolic disorders. Modulating ANGPTL7 activity through recombinant protein administration or targeted interventions may have significant implications for lipid metabolism, adipose tissue function, and insulin sensitivity. Exploring ANGPTL7 as a therapeutic target holds promise for the development of novel strategies to tackle metabolic disorders.
Conclusion:
ANGPTL7 is an emerging player in metabolic regulation with potential therapeutic implications for metabolic disorders. Its involvement in lipid metabolism, adipose tissue biology, and insulin signaling pathways highlights its importance in maintaining metabolic homeostasis. The availability of ANGPTL7 human recombinant protein opens up new possibilities for further investigations and the development of targeted interventions for metabolic disorders.
What is the molecular weight/Mw of ANGPTL7 Protein?
ANGPTL7 Protein has a total Mw of 63.2kDa.
What is the source or expression system of ANGPTL7 Protein?
HEK293 cells.
What is the Purity of ANGPTL7 Protein?
ANGPTL7 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ANGPTL7 Protein?
The biological functionality of ANGPTL7 Protein will be determined in the future.
What is the amino acid sequence of ANGPTL7 Protein?
QKLSKHKTPA QPQLKAANCC EEVKELKAQV ANLSSLLSEL NKKQERDWVS VVMQVMELES NSKRMESRLT DAESKYSEMN NQIDIMQLQA AQTVTQTSAD AIYDCSSLYQ KNYRISGVYK LPPDDFLGSP ELEVFCDMET SGGGWTIIQR RKSGLVSFYR DWKQYKQGFG SIRGDFWLGN EHIHRLSRQP TRLRVEMEDW EGNLRYAEYS HFVLGNELNS YRLFLGNYTG NVGNDALQYH NNTAFSTKDK DNDNCLDKCA QLRKGGYWYN CCTDSNLNGV YYRLGEHNKH LDGITWYGWH GSTYSLKRVE MKIRPEDFKP LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK
What applications can ANGPTL7 Protein be used in?
ANGPTL7 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ANGPTL7 Protein?
The endotoxin level is minimal, ANGPTL7 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ARMC10 HumanDescription:
Armadillo Repeat Containing 10 Human Recombinant
Armadillo repeat-containing protein 10, Splicing variant involved in hepatocarcinogenesis protein, ARMC10, SVH.
Product # :
PRO-1453Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ARMC10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (28-308 a.a) and having a molecular mass of 33.6 kDa.ARMC10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARMC10 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
AMRC10 is a protein which contains an armadillo repeat and transmembrane domain. Upregulation of the AMRC10 gene has a role in hepatocellular carcinoma. AMRC10 decreases the transcriptional activity of the tumor suppressor protein p53 through direct interaction with the DNA-binding domain of p53, moreover it might play a role in cell growth and survival.
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Synonyms
Armadillo repeat-containing protein 10, Splicing variant involved in hepatocarcinogenesis protein, ARMC10, SVH.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSTRGRRRG DRELGIRSSK SAEDLTDGSY DDVLNAEQLQ KLLYLLESTE DPVIIERALI TLGNNAAFSV NQAIIRELGG IPIVANKINH SNQSIKEKAL NALNNLSVNV ENQIKIKIYI SQVCEDVFSG PLNSAVQLAG LTLLTNMTVT NDHQHMLHSY ITDLFQVLLT GNGNTKVQVL KLLLNLSENP AMTEGLLRAQ VDSSFLSLYD SHVAKEILLR VLTLFQNIKN CLKIEGHLAV QPTFTEGSLF FLLHGEECAQ KIRALVDHHD AEVKEKVVTI IPKI.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TAGLN3 HumanDescription:
Transgelin-3 Human Recombinant
Transgelin 3, NP22, NP25, Neuronal protein 22, Neuronal protein NP25.
Product # :
PRO-946Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TAGLN3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (1-199) and having a molecular mass of 24.6 kDa.The TAGLN3 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TAGLN3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
TAGLN3 holds a putative Actin-binding domain, two potential phosphorylation sites, two EF-hand motifs and a calponin-homology (CH) domain. TAGLN3 is homologic to transgelin and calponin, two cytoskeleton-interacting proteins. TAGLN3 is a member of the calponin family, and is co-localized with Actin and tubulin, which indicates that TAGLN3 has a part in neuronal plasticity or as a signaling protein. As a result of a wide-ranging expression pattern, TAGLN3 is able to take different roles in the developing and adult brain.
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Synonyms
Transgelin 3, NP22, NP25, Neuronal protein 22, Neuronal protein NP25.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MANRGPSYGL SREVQEKIEQ KYDADLENKL VDWIILQCAE DIEHPPPGRA HFQKWLMDGT VLCKLINSLY PPGQEPIPKI SESKMAFKQM EQISQFLKAA ETYGVRTTDI FQTVDLWEGK DMAAVQRTLM ALGSVAVTKD DGCYRGEPSW FHRKAQQNRR GFSEEQLRQG QNVIGLQMGS NKGASQAGMT GYGMPRQIM
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.