Search: 1000 results found for "Stanniocalcin"

Description:

Granulocyte Macrophage-Colony Stimulating Factor Mouse Recombinant

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, CSF2, GMCSF

Product # :

CYT-222

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Description

Granulocyte Macrophage Colony Stimulating Factor Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids and having a molecular mass of 14285.35 Dalton.GM-CSF Mouse is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GM-CSF Mouse was lyophilized with no additives.

Purity

Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of the proliferation of murine FDC-P1 cell line is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.

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Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, CSF2, GMCSF
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GM-CSF 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.
Solubility
It is recommended to reconstitute the lyophilized Granulocyte Macrophage Colony Stimulating Factor in sterile 20mM AcOH (acetic Acid) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Thr-Arg.
Background
What is the molecular weight/Mw of GM-CSF MOUSE Protein?
GM-CSF MOUSE Protein has a total Mw of 14.28kDa.

What is the source or expression system of GM-CSF MOUSE Protein?
Escherichia Coli.

What is the Purity of GM-CSF MOUSE Protein?
GM-CSF MOUSE Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of GM-CSF MOUSE Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of murine FDC-P1 cell line is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.

What is the amino acid sequence of GM-CSF MOUSE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Thr-Arg.

What applications can GM-CSF MOUSE Protein be used in?
GM-CSF MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GM-CSF MOUSE Protein?
The endotoxin level is minimal, GM-CSF MOUSE Protein was purified using conventional chromatography techniques.
Protein content
GM-CSF quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.765 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 GM-CSF 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.

Description:

Serine/Threonine Kinase 16 Human Recombinant

Serine/threonine-protein kinase 16, Myristoylated and palmitoylated serine/threonine-protein kinase, MPSK, Protein kinase PKL12, TGF-beta-stimulated factor 1, TSF-1, Tyrosine-protein kinase STK16, hPSK, STK16, MPSK1, PKL12, TSF1, KRCT.

Product # :

PKA-032

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Description

STK16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 329 amino acids (1-305 a.a) and having a molecular mass of 37.2kDa.STK16 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

STK16 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Serine/threonine-protein kinase 16 (STK16) is a membrane-associated protein kinase which phosphorylates on serine and threonine residues. STK16 is involved in secretory vesicle trafficking or intracellular signaling. Furthermore, the STK16 protein may have a role in regulating stromal-epithelial interactions which occur during ductal morphogenesis in the mammary gland. STK16 can autophosphorylate on Tyr residue; it is however unclear whether STK16 has tyrosine-protein kinase toward other proteins. STK16 may also be involved in TGF-beta signaling.
Synonyms
Serine/threonine-protein kinase 16, Myristoylated and palmitoylated serine/threonine-protein kinase, MPSK, Protein kinase PKL12, TGF-beta-stimulated factor 1, TSF-1, Tyrosine-protein kinase STK16, hPSK, STK16, MPSK1, PKL12, TSF1, KRCT.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMGHALC VCSRGTVIID NKRYLFIQKL GEGGFSYVDL VEGLHDGHFY ALKRILCHEQ QDREEAQREA DMHRLFNHPN ILRLVAYCLR ERGAKHEAWL LLPFFKRGTL WNEIERLKDK GNFLTEDQIL WLLLGICRGL EAIHAKGYAH RDLKPTNILL GDEGQPVLMD LGSMNQACIH VEGSRQALTL QDWAAQRCTI SYRAPELFSV QSHCVIDERT DVWSLGCVLY AMMFGEGPYD MVFQKGDSVA LAVQNQLSIP QSPRHSSALR QLLNSMMTVD PHQRPHIPLL LSQLEALQPP APGQHTTQI.

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.

Description:

Stomatin Human Recombinant

BND7, EPB7, EPB72, Erythrocyte band 7 integral membrane protein, Protein 7.2b, Stomatin, STOM.

Product # :

PRO-1525

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Description

STOM Human Recombinant produced in E. coli is a single polypeptide chain containing 257 amino acids (55-288) and having a molecular mass of 28 kDa. STOM is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The STOM solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Stomatin (STOM) is a part of a highly conserved family of integral membrane proteins. STOM is a membrane protein involved in regulation of monovalent cation transport through lipid membranes which regulates ACCN1 and ACCN3 gating. STOM is a major lipid-raft component of erythrocytes and epithelial cells, and an abundant platelet protein which acts as a cytoskeletal anchor.
Synonyms
BND7, EPB7, EPB72, Erythrocyte band 7 integral membrane protein, Protein 7.2b, Stomatin, STOM.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSKIIKEYE RAIIFRLGRI LQGGAKGPGL FFILPCTDSF IKVDMRTISF DIPPQEILTK DSVTISVDGV VYYRVQNATL AVANITNADS ATRLLAQTTL RNVLGTKNLS QILSDREEIA HNMQSTLDDA TDAWGIKVER VEIKDVKLPV QLQRAMAAEA EASREARAKV IAAEGEMNAS RALKEASMVI TESPAALQLR YLQTLTTIAA EKNSTIVFPL PIDMLQGIIG AKHSHLG.

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.

Description:

Plasminogen Activator Inhibitor-1 Human Recombinant

PAI-1, PAI1, PLANH1, SERPINE1, PAIE, PLASMINOGEN ACTIVATOR INHIBITOR, BETA-MIGRATING ENDOTHELIAL-CELL-DERIVED TYPE.

Product # :

ENZ-357

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Description

SERPINE1 Human Recombinant fused to an N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 400 amino acids (24-402) and having a molecular mass of 45kDa.SERPINE1 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

50mM NaAc (pH 5.5), 10% glycerol and 0.1M NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The IC50 for this effect is less than 3nM, measured by its ability to inhibit uPA cleavage of the substrate Z-GGRAMC.

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Introduction
Plasminogen activator inhibitor-1 is the principal inhibitor of tissue plasminogen activator(tPA) and uPA, the activators of plasminogenand hence fibrinolysis(the physiological breakdown of blood clots). It is a serine protease inhibitor(serpin) protein (SERPINE1). The other PAI, plasminogen activator inhibitor-2(PAI-2) is secreted by the placentaand only present in significant amounts during pregnancy. In addition, protease nexinacts as an inhibitor of tPA. SERPINE1, however, is the main inhibitor of the plasminogen activators.
Synonyms
PAI-1, PAI1, PLANH1, SERPINE1, PAIE, PLASMINOGEN ACTIVATOR INHIBITOR, BETA-MIGRATING ENDOTHELIAL-CELL-DERIVED TYPE.
Physical Appearance
Sterile Filtered clear 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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MVHHPPSYVA HLASDFGVRV FQQVAQASKD RNVVFSPYGVASVLAMLQLT TGGETQQQIQ AAMGFKIDDK GMAPALRHLY KELMGPWNKD EISTTDAIFVQRDLKLVQGF MPHFFRLFRS TVKQVDFSEV ERARFIINDW VKTHTKGMIS NLLGKGAVDQLTRLVLVNAL YFNGQWKTPF PDSSTHRRLF HKSDGSTVSV PMMAQTNKFN YTEFTTPDGHYYDILELPYH GDTLSMFIAA PYEKEVPLSA LTNILSAQLI SHWKGNMTRL PRLLVLPKFSLETEVDLRKP LENLGMTDMF RQFQADFTSL SDQEPLHVAQ ALQKVKIEVN ESGTVASSSTAVIVSARMAP EEIIMDRPFL FVVRHNPTGT VLFMGQVMEP.

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.

Description:

Astrovirus Capsid Recombinant

Product # :

ASR-001

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Description

Recombinant Astrovirus Capsid (50-450 aa) produced in E.coli and migrates at42-45kDa. The Astrovirus Capsid is fused to a 6xHis tag and purified by proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

Astrovirus Capsidprotein solution contains 25mM Tris Base and 10mM K2CO3.

Purity

Protein is >95% pure as determined by 10% PAGE (coomassie staining).

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Introduction
Astroviruses are the main cause of gastroenteritis in children and elderly adults. Astroviruses are associated with 5–9% of cases of gastroenteritis in young children. The virus is found in faecal matter and in epithelial intestinal cells. Astrovirus’s main transmission is by contaminated food or water.
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.
Applications
ELISA, Western blot.

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.

Description:

Stromal Cell-Derived Factor-1 alpha (CXCL12), Mouse Recombinant, His Tag

SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell stimulating factor, TLSF.

Product # :

CHM-323

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Description

SDF 1a Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 91 amino acids (22-89 a.a) and having a molecular mass of 10.4kDa. SDF 1a is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SDF 1a protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell stimulating factor, TLSF.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSKPVSLSY RCPCRFFESH IARANVKHLK ILNTPNCALQ IVARLKNNNR QVCIDPKLKW IQEYLEKALN K.
Background
What is the molecular weight/Mw of CXCL12 MOUSE ALPHA, HIS Protein?
CXCL12 MOUSE ALPHA, HIS Protein has a total Mw of 10.4kDa.

What is the source or expression system of CXCL12 MOUSE ALPHA, HIS Protein?
Escherichia Coli.

What is the Purity of CXCL12 MOUSE ALPHA, HIS Protein?
CXCL12 MOUSE ALPHA, HIS Protein is > 95% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL12 MOUSE ALPHA, HIS Protein?
The biological functionality of CXCL12 MOUSE ALPHA, HIS Protein will be determined in the future.

What is the amino acid sequence of CXCL12 MOUSE ALPHA, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSKPVSLSY RCPCRFFESH IARANVKHLK ILNTPNCALQ IVARLKNNNR QVCIDPKLKW IQEYLEKALN K.

What applications can CXCL12 MOUSE ALPHA, HIS Protein be used in?
CXCL12 MOUSE ALPHA, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL12 MOUSE ALPHA, HIS Protein?
The endotoxin level is minimal, CXCL12 MOUSE ALPHA, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL12 MOUSE ALPHA, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL12 MOUSE ALPHA, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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.

Description:

Nuclear Apoptosis Inducing Factor 1 Human Recombinant

bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.

Product # :

PRO-1978

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Description

NAIF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (1-327 a.a) and having a molecular mass of 37.6kDa. NAIF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

NAIF1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Nuclear Apoptosis Inducing Factor 1 (NAIF1) is a part of the NAIF1 family. NAIF1 Interacts with HARBI1 and Induces apoptosis.
Synonyms
bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAVPAKK RKMNFSEREV EIIVEELELK KHLLVNHFNA GVPLAAKSAA WHGILRRVNA VATCRRELPE VKKKWSDLKT EVRRKVAQVR AAVEGGEAPG PTEEDGAGGP GTGGGSGGGG PAVAPVLLTP MQQRICNLLG EATIISLPST TEIHPVALGP SATAAAATVT LTQIPTETTY HTLEEGVVEY CTAEAPPPLP PETPVDMMAQ HADTSVKPQA LKSRIALNSA KLIQEQRVTN LHVKEIAQHL EQQNDLLQMI RRSQEVQACA QERQAQAMEG TQAALSVLIQ VLRPMIKDFR RYLQSNTANP APASDPGQVA QNGQPDSIIQ.

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.

Description:

Annexin A8 Like-1 Human Recombinant

Annexin A8-like protein 2, bA145E20.2, ANXA8, annexin A8L2.

Product # :

PRO-1138

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Description

ANXA8L1 Human Recombinant produced in E. coli is a single polypeptide chain containing 351 amino acids (1-327) and having a molecular mass of 39.4 kDa.ANXA8L1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The ANXA8L1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Annexin A8-like 2 (ANXA8L2) belongs to the annexin family of calcium-dependent phospholipid binding proteins. Annexin family members are regulators of such varied processes such as ion flux, endocytosis and exocytosis, and cellular adhesion. ANXA8L2 is a membrane binding protein with various properties, including voltage-sensitive calcium channel activity, ion selectivity and membrane fusion. ANXA8L2 overexpressionis linked to acute myelocytic leukemia. ANXA8L2 may act as an anticoagulant which indirectly inhibits the thromboplastin-specific complex.
Synonyms
Annexin A8-like protein 2, bA145E20.2, ANXA8, annexin A8L2.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAWWKA WIEQEGVTVK SSSHFNPDPD AETLYKAMKG IGTNEQAIID VLTKRSNTQR QQIAKSFKAQ FGKDLTETLK SELSGKFERL IVALMYPPYR YEAKELHDAM KGLGTKEGVI IEILASRTKN QLREIMKAYE EDYGSSLEED IQADTSGYLE RILVCLLQGS RDDVSSFVDP ALALQDAQDL YAAGENIRGT DEMKFITILC TRSATHLLRV FEEYEKIANK SIEDSIKSET HGSLEEAMLT VVKCTQNLHS YFAERLYYAM KGAGTRDGTL IRNIVSRSEI DLNLIKCHFK KMYGKTLSSM IMEDTSGDYK NALLSLVGSD P

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.

Description:

Cyclin-Dependent Kinase 5 Human Recombinant,Sf9

CDK5, Cyclin Dependent Kinase 5, Serine/Threonine-Protein Kinase PSSALRE, Tau Protein Kinase II Catalytic Subunit, Cell Division Protein Kinase 5, TPKII Catalytic Subunit, Cyclin-Dependent-Like Kinase 5, Protein Kinase CDK5 Splicing, EC 2.7.11.22, EC 2.7.11.1, EC 2.7.11, PSSALRE, CDKN5, LIS7.

Product # :

PKA-104

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Description

CDK5 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 298 amino acids (1-292a.a.) and having a molecular mass of 34.1kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).CDK5 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

CDK5 protein solution (0.25mg/ml) Phosphate Buffered Saline (pH 7.4) containing 40% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Cell division protein kinase 5 (CDK5) belongs to the cyclin-dependent kinase family. CDK5 is essential for appropriate development of the brain and in order to be activated CDK5 must link to CDK5R1 or CDK5R2. CDK5 doesn't need phosphorylation on the T loop so that binding with the activator is enough to activate the kinase. CDK5 is engaged in the processes of neuronal maturation and migration, phosphorylating the central intracellular adaptor of the reeling signaling chain.
Synonyms
CDK5, Cyclin Dependent Kinase 5, Serine/Threonine-Protein Kinase PSSALRE, Tau Protein Kinase II Catalytic Subunit, Cell Division Protein Kinase 5, TPKII Catalytic Subunit, Cyclin-Dependent-Like Kinase 5, Protein Kinase CDK5 Splicing, EC 2.7.11.22, EC 2.7.11.1, EC 2.7.11, PSSALRE, CDKN5, LIS7.
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.
Amino Acid Sequence
MQKYEKLEKI GEGTYGTVFK AKNRETHEIV ALKRVRLDDD DEGVPSSALR EICLLKELKH KNIVRLHDVL HSDKKLTLVF EFCDQDLKKY FDSCNGDLDP EIVKSFLFQL LKGLGFCHSR NVLHRDLKPQ NLLINRNGEL KLADFGLARA FGIPVRCYSA EVVTLWYRPP DVLFGAKLYS TSIDMWSAGC IFAELANAGR PLFPGNDVDD QLKRIFRLLG TPTEEQWPSM TKLPDYKPYP MYPATTSLVN VVPKLNATGR DLLQNLLKCN PVQRISAEEA LQHPYFSDFC PPHHHHHH

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.

Description:

Interleukin 10 Human Recombinant, Sf9, Active

Interleukin-10, IL-10, Cytokine synthesis inhibitory factor, CSIF, IL10, GVHDS, IL10A, TGIF, T-Cell Growth Inhibitory Factor.

Product # :

CYT-1147

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Description

IL-10 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 166 amino acids (19-178 aa) and having a molecular mass of 19.4kDa. IL-10 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The IL-10 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using MC/9 mouse mast cells. The ED50 range < 5 ng/ml.

sds-page

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Introduction
Interleukin 10 or IL-10 or human cytokine synthesis inhibitory factor, is a cytokine (anti-inflammatory). IL10 gene is coding for il-10 In humans. Interleukin 10 has a receptor complex that is built from a couple of IL-10 receptor-1 and a couple of IL-10 receptor-2 proteins. therfore, the whole receptor unit consists of four IL-10 receptor molecules. IL-10 binds the receptor and causes STAT3 signalling through the phosphorylation of the cytoplasmic ends of IL-10 receptor 1 and IL-10 receptor 2 through JAK1 and Tyk2.
Synonyms
Interleukin-10, IL-10, Cytokine synthesis inhibitory factor, CSIF, IL10, GVHDS, IL10A, TGIF, T-Cell Growth Inhibitory Factor.
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.
Amino Acid Sequence
SPGQGTQSEN SCTHFPGNLP NMLRDLRDAF SRVKTFFQMK DQLDNLLLKE SLLEDFKGYL GCQALSEMIQ FYLEEVMPQA ENQDPDIKAH VNSLGENLKT LRLRLRRCHR FLPCENKSKA VEQVKNAFNK LQEKGIYKAM SEFDIFINYI EAYMTMKIRN HHHHHH.
Background
What is the molecular weight/Mw of IL10 HUMAN, SF9 Protein?
IL10 HUMAN, SF9 Protein has a total Mw of 19.4kDa.

What is the source or expression system of IL10 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of IL10 HUMAN, SF9 Protein?
IL10 HUMAN, SF9 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL10 HUMAN, SF9 Protein?
Measured in a cell proliferation assay using MC/9 mouse mast cells. The ED50 range < 5 ng/ml.

What is the amino acid sequence of IL10 HUMAN, SF9 Protein?
SPGQGTQSEN SCTHFPGNLP NMLRDLRDAF SRVKTFFQMK DQLDNLLLKE SLLEDFKGYL GCQALSEMIQ FYLEEVMPQA ENQDPDIKAH VNSLGENLKT LRLRLRRCHR FLPCENKSKA VEQVKNAFNK LQEKGIYKAM SEFDIFINYI EAYMTMKIRN HHHHHH.

What applications can IL10 HUMAN, SF9 Protein be used in?
IL10 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL10 HUMAN, SF9 Protein?
The endotoxin level is minimal, IL10 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL10 HUMAN, SF9 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL10 HUMAN, SF9?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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.

Description:

Transferrin Receptor Human Recombinant, Sf9

Transferrin Receptor, P90, T9, TR, Transferrin Receptor (P90, CD71), Transferrin Receptor Protein 1, CD71 Antigen, IMD46, CD71, TFR1.

Product # :

PRO-2587

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Description

TFRC produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 669 amino acids (101-760a.a.) and having a molecular mass of 74.9kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). TFRC is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques

Source

Sf9, Baculovirus cells.

Formulation

TFRC 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.

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Introduction
The Transferrin glycoproteins are responsible for the blood levels of free iron by binding to iron in the plasma. The transferrin molecules in humans are encoded by a gene called TF. Transferrin binds to iron in a tight but reversible way. The iron levels that binds to transferrin are very low in comparison to the total body iron, nonetheless, it is extremely vital iron levels with the greatest turnover rate.
Synonyms
Transferrin Receptor, P90, T9, TR, Transferrin Receptor (P90, CD71), Transferrin Receptor Protein 1, CD71 Antigen, IMD46, CD71, TFR1.
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.
Amino Acid Sequence
ADPLAGTESP VREEPGEDFP AARRLYWDDL KRKLSEKLDS TDFTGTIKLL NENSYVPREA GSQKDENLAL Recombinant Human TFRC Protein Catalog Number: ATGP3825 YVENQFREFK LSKVWRDQHFVKIQVKDSAQ NSVIIVDKNG RLVYLVENPG GYVAYSKAAT VTGKLVHANF GTKKDFEDLY TPVNGSIVIV RAGKITFAEK VANAESLNAI GVLIYMDQTK FPIVNAELSF FGHAHLGTGD PYTPGFPSFN HTQFPPSRSS GLPNIPVQTI SRAAAEKLFG NMEGDCPSDW KTDSTCRMVTSESKNVKLTV SNVLKEIKIL NIFGVIKGFV EPDHYVVVGA QRDAWGPGAA KSGVGTALLL KLAQMFSDMV LKDGFQPSRS IIFASWSAGD FGSVGATEWL EGYLSSLHLK AFTYINLDKA VLGTSNFKVS ASPLLYTLIE KTMQNVKHPV TGQFLYQDSN WASKVEKLTL DNAAFPFLAYSGIPAVSFCF CEDTDYPYLG TTMDTYKELI ERIPELNKVA RAAAEVAGQF VIKLTHDVEL NLDYERYNSQ LLSFVRDLNQ YRADIKEMGL SLQWLYSARG DFFRATSRLT TDFGNAEKTD RFVMKKLNDR VMRVEYHFLS PYVSPKESPF RHVFWGSGSH TLPALLENLK LRKQNNGAFNETLFRNQLAL ATWTIQGAAN ALSGDVWDID NEFHHHHHH.

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.

Description:

Kallikrein-2 Human Recombinant, sf9

hK2, KLK2A2, Kallikrein-2, Glandular kallikrein-1, hGK-1, issue kallikrein-2, KLK2.

Product # :

ENZ-971

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Description

KLK2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 246 amino acids (25-261 aa) and having a molecular mass of 27.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).KLK2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

KLK2 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
KLK2 is a part of the grandular kallikrein protein family whose Members are engaged in a diverse array of biological functions. Kallikreins are a subgroup of serine proteases which are clustered on chromosome 19. KLK2 is a highly active trypsin-like serine protease which selectively cleaves at arginine remains. KLK2 is mostly expressed in prostatic tissue and is accountable for cleaving pro-prostate-specific antigen into its enzymatically active form. KLK2 is greatly expressed in prostate tumor cells and may possibly be a prognostic maker for prostate cancer risk.
Synonyms
hK2, KLK2A2, Kallikrein-2, Glandular kallikrein-1, hGK-1, issue kallikrein-2, KLK2.
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.
Amino Acid Sequence
ADPIVGGWEC EKHSQPWQVA VYSHGWAHCG GVLVHPQWVL TAAHCLKKNS QVWLGRHNLF EPEDTGQRVP VSHSFPHPLY NMSLLKHQSL RPDEDSSHDL MLLRLSEPAK ITDVVKVLGL PTQEPALGTT CYASGWGSIE PEEFLRPRSL QCVSLHLLSN DMCARAYSEK VTEFMLCAGL WTGGKDTCGG DSGGPLVCNG VLQGITSWGP EPCALPEKPA VYTKVVHYRK WIKDTIAANP HHHHHH

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.

Description:

Troponin I Type 2 Human Recombinant, His Tag

AMCD2B, DA2B, FSSV, fsTnI, Troponin I, fast skeletal muscle, Troponin I, fast-twitch isoform.

Product # :

PRO-1283

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Description

TNNI2 Human Recombinant produced in E. coli is a single polypeptide chain containing 202 amino acids (1-182) and having a molecular mass of 23.5 kDa. TNNI2 is fused to 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The TNNI2 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea, 20% glycerol and 0.2M NaCl.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Troponin I, fast skeletal muscle (TNNI2), belongs to the troponin I gene family, and a part of the troponin complex including troponin T, troponin C and troponin I subunits. The troponin complex, along with tropomyosin, is responsible for the calcium-dependent regulation of striated muscle contraction. TNNI2 is also suppresses tumor growth in human ovarian carcinoma. Mutations in TNNI2 cause myopathy and distal arthrogryposis type 2B.
Synonyms
AMCD2B, DA2B, FSSV, fsTnI, Troponin I, fast skeletal muscle, Troponin I, fast-twitch isoform.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGDEEKRNRA ITARRQHLKS VMLQIAATEL EKEESRREAE KQNYLAEHCP PLHIPGSMSE VQELCKQLHA KIDAAEEEKY DMEVRVQKTS KELEDMNQKL FDLRGKFKRP PLRRVRMSAD AMLKALLGSK HKVCMDLRAN LKQVKKEDTE KERDLRDVGD WRKNIEEKSG MEGRKKMFES ES.

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.

Description:

Soluble CD23 Human Recombinant

Low affinity immunoglobulin epsilon Fc receptor, Lymphocyte IgE receptor, Fc-epsilon-RII, BLAST-2, Immunoglobulin E-binding factor, CD23 antigen, FCER2, CD23, FCE2, CD23A, IGEBF, CLEC4J.

Product # :

PRO-1789

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Quantity :

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Shipped at Room temp

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Description

sCD23 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids and having a molecular mass of 19.2kDa.The sCD23 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 is determined by its ability to induce TNF-alpha production by human PBMCs.

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Introduction
CD23 is a 45kDa glycoprotein, which is present on a subpopulation of freshly isolated peripheral blood and tonsil B cells and strongly expressed on EBV-transformed B lymphoblasts. The CD23 molecule is identical to the low affinity IgE receptor found on B cells. Expression of CD23 has been detected in neoplastic cells from cases of B cell chronic lymphocyctic leukaemia and some cases of centroblastic/centrocytic lymphoma.
Synonyms
Low affinity immunoglobulin epsilon Fc receptor, Lymphocyte IgE receptor, Fc-epsilon-RII, BLAST-2, Immunoglobulin E-binding factor, CD23 antigen, FCER2, CD23, FCE2, CD23A, IGEBF, CLEC4J.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized sCD23 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution sCD23 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.
Solubility
It is recommended to reconstitute the lyophilized sCD23 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MELQVSSGFV CNTCPEKWIN FQRKCYYFGK GTKQWVHARY ACDDMEGQLV SIHSPEEQDF LTKHASHTGS WIGLRNLDLK GEFIWVDGSH VDYSNWAPGE PTSRSQGEDC VMMRGSGRWN DAFCDRKLGA WVCDRLATCT PPASEGSAES MGPDSRPDPD GRLPTPSAPL HS

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.

Description:

Intercellular Adhesion Molecule-1 Human Recombinant, SF9

Intercellular Adhesion Molecule 1, Major Group Rhinovirus Receptor, ICAM-1, Intercellular Adhesion Molecule 1 (CD54), Human Rhinovirus Receptor, Cell Surface Glycoprotein P3.58, Human Rhinovirus Receptor, CD54 Antigen, P3.58, CD54, BB2, Intercellular adhesion molecule 1.

Product # :

PRO-2200

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Description

ICAM1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 692 amino acids (28-480a.a.) and having a molecular mass of 76.5kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). ICAM1 is expressed with a 239 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

ICAM1 protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The ED50 range ≤ 2 ug/ml is measured by the ability of the immobilized protein to support the adhesion of HL-60 human promyelocytic cells. When cells are added to Human ICAM-1/CD54 coated plates.

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Introduction
ICAM-1 also called CD54 is a single chain membrane glycoprotein expressed on the surface of a variety of non-haematopoietic and haematopoietic cell types and has roles in signal transduction, cell signaling and lymphocyte adhesion. ICAM1 binds to integrins such as CD11a / CD18, or CD11b / CD18. ICAM1 is also used by Rhinovirus as a receptor. ICAM-1 is an intercellular adhesion molecule constantly present in low concentrations in the membranes of leukocytes and endothelial cells. When stimulated by cytokine the concentrations significantly increase. ICAM-1 can be stimulated by interleukin-1 (IL-1) and tumor necrosis factor alpha (TNFA) and is expressed by the vascular endothelium, macrophages and lymphocytes. ICAM-1 is a ligand for LFA-1 which is a receptor found on leukocytes. Upon activation, leukocytes bind to endothelial cells via ICAM-1/LFA-1 and then transmigrate into tissues. ICAM-1 is implicated in subarachnoid hemorrhage (SAH). Levels of ICAM-1 are shown to be notably elevated in patients with SAH. Soluble ICAM-1 is detectable in the plasma and is elevated in patients with various inflammatory conditions.
Synonyms
Intercellular Adhesion Molecule 1, Major Group Rhinovirus Receptor, ICAM-1, Intercellular Adhesion Molecule 1 (CD54), Human Rhinovirus Receptor, Cell Surface Glycoprotein P3.58, Human Rhinovirus Receptor, CD54 Antigen, P3.58, CD54, BB2, Intercellular adhesion molecule 1.
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.
Amino Acid Sequence
QTSVSPSKVI LPRGGSVLVT CSTSCDQPKL LGIETPLPKK ELLLPGNNRK VYELSNVQED SQPMCYSNCP DGQSTAKTFL TVYWTPERVE LAPLPSWQPV GKNLTLRCQV EGGAPRANLT VVLLRGEKEL KREPAVGEPA EVTTTVLVRR DHHGANFSCR TELDLRPQGL ELFENTSAPY QLQTFVLPAT PPQLVSPRVL EVDTQGTVVC SLDGLFPVSE AQVHLALGDQ RLNPTVTYGN DSFSAKASVS VTAEDEGTQR LTCAVILGNQ SQETLQTVTI YSFPAPNVIL TKPEVSEGTE VTVKCEAHPR AKVTLNGVPA QPLGPRAQLL LKATPEDNGR SFSCSATLEV AGQLIHKNQT RELRVLYGPR LDERDCPGNW TWPENSQQTP MCQAWGNPLP ELKCLKDGTF PLPIGESVTV TRDLEGTYLC RARSTQGEVT REVTVNVLSP RYEVEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYRQKSL SLSPGKHHHH HH.
Background
Intercellular adhesion molecule-1 (ICAM-1) is a cell surface glycoprotein that plays a pivotal role in immune responses and inflammatory processes. This research aims to investigate the function and significance of ICAM-1 protein in various physiological and pathological conditions. Understanding the molecular mechanisms and regulatory roles of ICAM-1 can provide valuable insights into its potential as a therapeutic target for immune-related disorders.
Structure and Expression of ICAM-1 Protein:
ICAM-1 belongs to the immunoglobulin superfamily and is composed of five immunoglobulin-like domains. It is primarily expressed on the surfaces of endothelial cells, leukocytes, and other immune cells. ICAM-1 expression can be induced by pro-inflammatory cytokines, such as tumor necrosis factor-alpha (TNF-α) and interleukin-1 (IL-1), during immune responses and inflammatory conditions.
ICAM-1 and Leukocyte Adhesion:
One of the critical functions of ICAM-1 is its involvement in leukocyte adhesion and migration. ICAM-1 interacts with its primary receptor, lymphocyte function-associated antigen-1 (LFA-1), expressed on leukocytes. This interaction facilitates the firm adhesion of leukocytes to endothelial cells, leading to their transmigration into inflamed tissues. The ICAM-1/LFA-1 axis plays a crucial role in immune surveillance, inflammation, and host defense against pathogens.
Implications of ICAM-1 in Inflammatory Disorders:
ICAM-1 has been implicated in various inflammatory diseases, including rheumatoid arthritis, inflammatory bowel disease, and multiple sclerosis. Enhanced expression of ICAM-1 on endothelial cells promotes leukocyte recruitment and contributes to the perpetuation of chronic inflammation. Therefore, targeting ICAM-1-mediated leukocyte adhesion has emerged as a potential therapeutic strategy to alleviate inflammation and attenuate disease progression.
ICAM-1 in Viral Infections:
ICAM-1 also plays a role in viral infections, as several viruses exploit ICAM-1 to facilitate their entry into host cells. For instance, rhinoviruses, which cause the common cold, utilize ICAM-1 as a receptor for attachment and entry into respiratory epithelial cells. The interaction between ICAM-1 and viral proteins promotes viral internalization and subsequent infection. Understanding the mechanisms of ICAM-1-mediated viral entry can aid in the development of antiviral strategies.
Therapeutic Targeting of ICAM-1:
Given its crucial involvement in immune responses and disease pathogenesis, ICAM-1 has emerged as a potential therapeutic target. Strategies aimed at blocking ICAM-1/LFA-1 interactions have shown promise in preclinical and clinical studies. Monoclonal antibodies targeting ICAM-1 or LFA-1 have been developed to prevent leukocyte adhesion and reduce inflammation. Additionally, small molecule inhibitors and gene therapies targeting ICAM-1 expression are being explored as potential therapeutic interventions.
Challenges and Future Directions:
Although therapeutic targeting of ICAM-1 shows promise, several challenges need to be addressed. Specific targeting of ICAM-1 without affecting its physiological functions and potential off-target effects are important considerations. Additionally, the complex and dynamic nature of ICAM-1 expression and regulation require further investigation to optimize therapeutic strategies.
Conclusion:
The investigation of ICAM-1 protein provides insights into its pivotal role in immune responses, leukocyte adhesion, and inflammatory processes. Understanding the molecular mechanisms and functional implications of ICAM-1 opens avenues for the development of targeted therapies for inflammatory disorders and viral infections. Further research on ICAM-1 protein

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.

Description:

Interleukin-7 Human Recombinant, sf9

Interleukin 7, IL-7, Interleukin-7.

Product # :

CYT-975

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Description

IL7 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 161 amino acids (26-177 a.a.) and having a molecular mass of 18.4kDa. IL7 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL7 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.

SDS-PAGE

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Introduction
IL-7 is a cytokine important for B and T cell development. This cytokine and the hepatocyte growth factor (HGF) form a heterodimer that functions as a pre-pro-B cell growth-stimulating factor. This cytokine is found to be a cofactor for V(D)J rearrangement of the T cell receptor beta (TCRB) during early T cell development. This cytokine can be produced locally by intestinal epithelial and epithelial goblet cells, and may serve as a regulatory factor for intestinal mucosal lymphocytes. Knockout studies in mice suggested that this cytokine plays an essential role in lymphoid cell survival.
Synonyms
Interleukin 7, IL-7, Interleukin-7.
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.
Amino Acid Sequence
ADPDCDIEGK DGKQYESVLM VSIDQLLDSM KEIGSNCLNN EFNFFKRHIC DANKEGMFLF RAARKLRQFL KMNSTGDFDL HLLKVSEGTT ILLNCTGQVK GRKPAALGEA QPTKSLEENK SLKEQKKLND LCFLKRLLQE IKTCWNKILM GTKEHHHHHH H
Background
What is the molecular weight/Mw of IL7 HUMAN, SF9 Protein?
IL7 HUMAN, SF9 Protein has a total Mw of 18.4kDa.

What is the source or expression system of IL7 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of IL7 HUMAN, SF9 Protein?
IL7 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL7 HUMAN, SF9 Protein?
The biological functionality of IL7 HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of IL7 HUMAN, SF9 Protein?
ADPDCDIEGK DGKQYESVLM VSIDQLLDSM KEIGSNCLNN EFNFFKRHIC DANKEGMFLF RAARKLRQFL KMNSTGDFDL HLLKVSEGTT ILLNCTGQVK GRKPAALGEA QPTKSLEENK SLKEQKKLND LCFLKRLLQE IKTCWNKILM GTKEHHHHHH H.

What applications can IL7 HUMAN, SF9 Protein be used in?
IL7 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL7 HUMAN, SF9 Protein?
The endotoxin level is minimal, IL7 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL7 HUMAN, SF9 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL7 HUMAN, SF9?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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.

Description:

Allergen Fra e 1.0101 Recombinant

Allergen Fra e 1.0101, Fra e 1.0101, Fra e 1.

Product # :

PRO-2286

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Quantity :

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Description

Recombinant Allergen Fra e 1.0101 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 17,794 Dalton. Fra e 1.0101 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Sf9 insect cells.

Formulation

Fra e 1.0101 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Allergen Fra e 1.0101 (Fra e 1.0101) causes an allergic reaction in humans.
Synonyms
Allergen Fra e 1.0101, Fra e 1.0101, Fra e 1.
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. Avoid multiple freeze-thaw cycles.
Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
Molar extinction coefficient
14815; A280(1mg/ml)=0.833

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.

Description:

Caveolin-1, Mouse Anti Human

Caveolin-1, CAV1, CAV, CGL3, BSCL3, VIP21, MSTP085.

Product # :

ANT-027

Price :

Quantity :

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Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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Introduction
The scaffolding protein encoded by the CAV1 gene is the key component of the caveolae plasma membranes found in most cell types. Cholesterol is vital for caveolae formation and maintenance, and caveolae structure is highly sensitive to cholesterol depletion or treatment with cholesterol binding drugs. CAV1 can tightly and specifically bind free cholesterol and artificial cholesterol containing vesicles. Caveolin 1 links integrin subunits to the tyrosine kinase FYN, which is an initiating step in coupling integrins to the Ras-ERK pathway and promoting cell cycle progression. CAV1 is a tumor suppressor gene candidate and a negative regulator of the Ras-p42/44 mitogen-activated kinase. Caveolin 1 and caveolin 2 are positioned next to each other on chromosome 7 and express co-localizing proteins which form a stable hetero-oligomeric complex cascade. Mutations in the CAV1 gene are linked to Berardinelli-Seip congenital lipodystrophy.
Synonyms
Caveolin-1, CAV1, CAV, CGL3, BSCL3, VIP21, MSTP085.
Physical Appearance
Sterile Filtered clear solution.
Immunogen
Anti-human CAV1 mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CAV1 amino acids 1-104 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and k light chain.
Clone
PAT4C1AT.
Applications
CAV1 antibody has been tested by ELISA, Western blot to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:250 ~ 1000.
Recommended starting dilution is 1:500.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
CAV1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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.

Description:

Coronavirus 2019 Nucleocapsid Mosaic Recombinant

Product # :

SARS-015

Price :

Quantity :

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Description

The E.Coli derived recombinant protein contains the Coronavirus 2019 full length nuclepocapsid Mosaic immunodominant regions [ full length N-antigen ], fused to 6xHis tag at C-terminal.

Source

Escherichia Coli.

Formulation

CoV 2019 Nucleocapsid-Mosaic Protein solution is supplied in 1x PBS.

Purity

CoV 2019 Nucleocapsid-Mosaic Protein ein is >90% pure as determined SDS-PAGE.

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Introduction
A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.
The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.
While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.
Physical Appearance
Sterile Filtered clear solution.
Stability
CoV 2019 Nucleocapsid-Mosaic Protein is shipped on ice packs. Upon arrival, Store at -20°C.
Specificity
Reactivity with SARS infected individuals not tested.

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.

Description:

Galanin Prepropeptide Human Recombinant

GALN, GLNN, GMAP, GAL, GAL1.

Product # :

PRO-1433

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Shipped with Ice Packs

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Description

GAL Human Recombinant produced in E. coli is a single polypeptide chain containing 127 amino acids (20-123) and having a molecular mass of 13.9kDa. GAL is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The GAL solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Galanin Prepropeptide (GAL) which is localized in brain pathways is involved in both cognition and affect, and also inhibits learning and memory by inhibiting neurotransmitter release and neuronal firing rate. GAL is a part of the galanin family and modulates a variety of physiological processed including cognition/memory, sensory/pain processing, neurotransmitter/hormone secretion, and feeding behavior. Galanin Prepropeptide is upregulated in primary afferent and sympathetic neurones and is required for the development of sympathetic perineuronal baskets subsequent to nerve injury.
Synonyms
GALN, GLNN, GMAP, GAL, GAL1.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSASAGLWS PAKEKRGWTL NSAGYLLGPH AVGNHRSFSD KNGLTSKREL RPEDDMKPGS FDRSIPENNI MRTIIEFLSF LHLKEAGALD RLLDLPAAASSEDIERS.

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.

Description:

Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant, Sf9

CSF-2, MGI-1GM, GMCSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

Product # :

CYT-416

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

GM-CSF Human Recombinant produced in insect cells is a single, glycosylated, polypeptide chain containing 127 amino acids (18-144) and having a molecular mass of 14.6kDa. GM-CSF is fused to a C-terminal His -tag (6x His) and purified by proprietary chromatographic techniques.

Source

Insect Cells.

Formulation

The protein was lyophilized with PBS.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

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Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
Synonyms
CSF-2, MGI-1GM, GMCSF, Pluripoietin-alpha, Molgramostin, Sargramostim.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF 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.
Solubility
It is recommended to reconstitute the lyophilized Granulocyte Macrophage Colony Stimulating Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.
Background
Recombinant Granulocyte-Macrophage Colony-Stimulating Factor (GMCSF) is a protein that plays a crucial role in the production and differentiation of white blood cells, including granulocytes and macrophages. It is a potent stimulator of hematopoietic stem cells, which are responsible for the production of all blood cells in the body. Recombinant GMCSF is a synthetic version of the protein that is produced using recombinant DNA technology.
Recombinant GMCSF has been extensively studied for its potential therapeutic applications in a variety of medical conditions, including cancer, autoimmune diseases, and infectious diseases. In cancer, GMCSF is used as an immunostimulatory agent to enhance the immune response against cancer cells. By stimulating the production and differentiation of white blood cells, GM-CSF can increase the number of immune cells that can recognize and attack cancer cells. This approach has been successfully used in the treatment of several types of cancer, including melanoma and leukemia.
In autoimmune diseases, recombinant GMCSF has been investigated as a potential treatment for conditions such as rheumatoid arthritis and multiple sclerosis. These diseases are characterized by an overactive immune response that attacks healthy tissues in the body. By modulating the immune response, GMCSF may be able to reduce inflammation and prevent further damage to affected tissues.
In infectious diseases, recombinant GMCSF has been studied as a potential treatment for conditions such as sepsis and HIV/AIDS. In sepsis, a severe bacterial infection, GMCSF may be able to stimulate the production of white blood cells and improve the immune response against the infection. In HIV/AIDS, GMCSF may be able to enhance the immune response against the virus and reduce the risk of opportunistic infections.
Recombinant GMCSF is typically administered by injection, either directly into the affected tissue or into the bloodstream. It is generally well-tolerated, although some patients may experience side effects such as fever, fatigue, and muscle pain.
In conclusion, recombinant GMCSF is a promising therapeutic agent with potential applications in a variety of medical conditions. Its ability to stimulate the production and differentiation of white blood cells makes it a valuable tool in the treatment of cancer, autoimmune diseases, and infectious diseases. Ongoing research is likely to uncover new uses for this protein and further refine its therapeutic potential.
What is the molecular weight/Mw of GM- CSF HUMAN, SF9 Protein?
GM- CSF HUMAN, SF9 Protein has a total Mw of 14.6kDa.

What is the source or expression system of GM- CSF HUMAN, SF9 Protein?
Insect Cells.
What is the Purity of GM- CSF HUMAN, SF9 Protein?
GM- CSF HUMAN, SF9 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of GM- CSF HUMAN, SF9 Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

What is the amino acid sequence of GM- CSF HUMAN, SF9 Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.

What applications can GM- CSF HUMAN, SF9 Protein be used in?
GM- CSF HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GM- CSF HUMAN, SF9 Protein?
The endotoxin level is minimal, GM- CSF HUMAN, SF9 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.

Description:

TROVE Domain Family Member 2 Human Recombinant, Biotinlyated

60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.

Product # :

PRO-2561

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

TROVE2 is a biotinlyated natural protein having a molecular mass of 58kDa. TROVE2 is purified from bovine tissues by protein-chemical methods.

Source

Bovine tissues.

Formulation

TROVE2 is supplied in 20mM HEPES buffer pH-8.0, 150mM NaCl and 20% glycerol.

Purity

Greater than 83.0% as determined by SDS-PAGE.

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Introduction
Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.
Synonyms
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
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. Avoid multiple freeze-thaw cycles.

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.

Description:

Cyclin-Dependent Kinase Inhibitor 1A (20-149 a.a.) Human Recombinant

Cyclin-Dependent Kinase Inhibitor 1A (P21, Cip1), Melanoma Differentiation Associated Protein 6, Wild-Type P53-Activated Fragment 1, CDK-Interaction Protein 1, DNA Synthesis Inhibitor, CDK-Interacting Protein 1, CDKN1, P21Cip1/Waf1, MDA6, P21CIP1, CAP20, WAF1, CIP1, PIC1, P21, SDI1.

Product # :

PKA-137

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

The CDKN1A Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The CDKN1A His-Tagged Fusion Protein, produced in E. coli, is a 20kDa protein containing 130 amino acid residues of the CDKN1A Human, 20-149 amino acids.

Source

Escherichia Coli.

Formulation

Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Synonyms
Cyclin-Dependent Kinase Inhibitor 1A (P21, Cip1), Melanoma Differentiation Associated Protein 6, Wild-Type P53-Activated Fragment 1, CDK-Interaction Protein 1, DNA Synthesis Inhibitor, CDK-Interacting Protein 1, CDKN1, P21Cip1/Waf1, MDA6, P21CIP1, CAP20, WAF1, CIP1, PIC1, P21, SDI1.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized CDKN1A at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Amino Acid Sequence
LFGPVDSEQL SRDCDALMAG CIQEARERWN FDFVTETPLEGDFAWERVRG LGLPKLYLPT GPRRGRDELG GGRRPGTSPA LLQGTAEEDH VDLSLSCTLVPRSGEQAEGS PGGPGDSQGR KRRQTSMTDF
Background
CDKN1A gene in humans plays an important role in maintaining genomic stability which is critical to cancer prevention and proper function of regular cellular processes. CDKN1A plays a main role in the cellular response to DNA mutation. CDKN1A overexpression causes cell cycle to stop. CDKN1A, along with CDK2 complexes aids to prevent kinase activity and inhibits progression through G1/S. CDKN1A can additionally increase assembly and activity in complexes of CDK4 or CDK6 and cyclin D.

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.

Description:

Interleukin-5 Mouse Recombinant, Sf9

interleukin 5, Il, Il-5, B-cell growth factor II, BCGF-II, Cytotoxic T-lymphocyte inducer, Eosinophil differentiation factor, T-cell replacing factor, EDF, TRF, B cell differentiation factor I, IL5.

Product # :

CYT-1195

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

IL5 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 119 amino acids (21-133 a.a) and having a molecular mass of 13.9kDa.IL5 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The IL5 solution (0.25mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 1 ng/ml.

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Introduction
The protein encoded by this gene is a cytokine that acts as a growth and differentiation factor for both B cells and eosinophils. IL5is a main regulator of eosinopoiesis, eosinophil maturation and activation. The elevated production of IL5is reported to be related to asthma or hypereosinophilic syndromes. The receptor of IL5is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). IL5, together with those for interleukin 4 (IL4), interleukin 13 (IL13), and CSF2, form a cytokine gene cluster on chromosome 5. IL5, IL4, and IL13 are found to be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31.
Synonyms
interleukin 5, Il, Il-5, B-cell growth factor II, BCGF-II, Cytotoxic T-lymphocyte inducer, Eosinophil differentiation factor, T-cell replacing factor, EDF, TRF, B cell differentiation factor I, IL5.
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.
Amino Acid Sequence
MEIPMSTVVK ETLTQLSAHR ALLTSNETMR LPVPTHKNHQ LCIGEIFQGL DILKNQTVRG GTVEMLFQNL SLIKKYIDRQ KEKCGEERRR TRQFLDYLQE FLGVMSTEWA MEGHHHHHH
Background
What is the molecular weight/Mw of IL 5 MOUSE, SF9 Protein?
IL 5 MOUSE, SF9 Protein has a total Mw of 13.9kDa.

What is the source or expression system of IL 5 MOUSE, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of IL 5 MOUSE, SF9 Protein?
IL 5 MOUSE, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 5 MOUSE, SF9 Protein?
Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 1 ng/ml.

What is the amino acid sequence of IL 5 MOUSE, SF9 Protein?
MEIPMSTVVK ETLTQLSAHR ALLTSNETMR LPVPTHKNHQ LCIGEIFQGL DILKNQTVRG GTVEMLFQNL SLIKKYIDRQ KEKCGEERRR TRQFLDYLQE FLGVMSTEWA MEGHHHHHH.

What applications can IL 5 MOUSE, SF9 Protein be used in?
IL 5 MOUSE, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 5 MOUSE, SF9 Protein?
The endotoxin level is minimal, IL 5 MOUSE, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 5 MOUSE, SF9 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL 5 MOUSE, SF9?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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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