Search: 1000 results found for "Anti Mouse Cytokine"

Description:

Lymphotactin (XCL1) Rat Recombinant

XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.

Product # :

CHM-038

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Description

Lymphotactin (XCL1) Rat Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of approximately 10.0kDa.Lymphotactin 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 as determined by a chemotaxis bioassay using human XCR1 transfected murine BaF3 cells < 100 ng/ml, corresponding to a specific activity of > 1.0 × 10⁴ IU/mg.

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Introduction
XCL1 is a small cytokine belongs to the XC chemokine family that is also known as lymphotactin. XCL1 is found in high levels in spleen, thymus, intestine and peripheral blood leukocytes, and at lower levels in lung, prostate gland and ovary. Cellular sources for XCL1 include activated thymic and peripheral blood CD8+ T cells. This chemokine attracts T cells. In humans, XCL1 is closely related to XCL2, whose gene is found at the same locus on chromosome 1. XCL1 induces it chemotactic function by binding to a chemokine receptor called XCR1.
Synonyms
XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized XCL1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Lymphotactin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Lymphotactin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VGTEVLQESI CVSLRTQRLP VQKIKTYTIK EGAMRAVIFV TKRGLRICAD PQAKWVKTAI KTVDGRASAS KSKAETIPTQ AQRSASTAVT LTG.

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:

HVEM Human Recombinant, His Tag

Tumor Necrosis Factor Receptor Superfamily Member 14, HVEM, TR2, Herpes Virus Entry Mediator A, Tumor Necrosis Factor Receptor-Like 2, Herpesvirus Entry Mediator, HVEA, ATAR, CD270, LIGHTR, CD40-Like Protein, Tumor Necrosis Factor Receptor-Like Gene2.

Product # :

CYT-800

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Description

TNFRSF14 Human Recombinant produced in E. Coli is a single, glycosylated polypeptide chain containing 187 amino acids (39-202) and having a molecular mass of 19.7kDa.TNFRSF14 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The TNFRSF14 solution (0.5mg/ml) containing 20mM Tris-HCl (pH 8.0), 0.1M NaCl and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
TNFRSF14, a member of the TNF receptor superfamily, is a type I transmembrane protein. TNFRSF14 is expressed in peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells. TNFRSF14 operates as a co-stimulatory factor for the activation of lymphoid cells and as a deterrent to infection by herpesvirus. Additionally, TNFRSF14 encourages the proliferation of T cells, and triggers apoptosis of various tumor cells.
Synonyms
Tumor Necrosis Factor Receptor Superfamily Member 14, HVEM, TR2, Herpes Virus Entry Mediator A, Tumor Necrosis Factor Receptor-Like 2, Herpesvirus Entry Mediator, HVEA, ATAR, CD270, LIGHTR, CD40-Like Protein, Tumor Necrosis Factor Receptor-Like Gene2.
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 MGSLPSCKED EYPVGSECCP KCSPGYRVKE ACGELTGTVC EPCPPGTYIA HLNGLSKCLQ CQMCDPAMGL RASRNCSRTE NAVCGCSPGH FCIVQDGDHC AACRAYATSS PGQRVQKGGT ESQDTLCQNC PPGTFSPNGT LEECQHQTKC SWLVTKAGAG TSSSHWV.

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:

TRAIL / APO2 Ligand Human Recombinant

Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.

Product # :

CYT-443

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Description

TRAIL/APO 2 Ligand Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 168 amino acids (Met+Arg115-Gly281) and having a molecular mass of ~21kDa. The sTRAIL is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a filtered (0.2µm) solution containing 20mM Tris-HCl pH 8.0 and 150mM NaCl.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The activity is determined by the cytolysis of Murine L929 cells in the presence of Actinomycin D, ED₅₀ for this effect is less than 2ng/ml, corresponding to a specific activity of 5,000,000IU/mg.

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Introduction
TNF-related apoptosis-inducing ligand (TRAIL) is a ligand molecule which induces apoptosis. It is a type II transmembrane protein with homology to other members of the tumor necrosis factor family.
In humans, the gene that encodes for TRAIL is located at chromosome 3q26. TRAIL binds to the death receptors, DR4 and DR5. The process of apoptosis is caspase-8-dependent. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues.
Synonyms
Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized APO 2 Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TRAIL 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 TRAIL in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MRERGPQRVA AHITGTRGRS NTLSSPNSKN EKALGRKINS WESSRSGHSF LSNLHLRNGE LVIHEKGFYY IYSQTYFRFQ EEIKENTKND KQMVQYIYKY TSYPDPILLM KSARNSCWSK DAEYGLYSIY QGGIFELKEN DRIFVSVTNE HLIDMDHEAS FFGAFLVG.

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:

Macrophage-Colony Stimulating Factor Rat Recombinant

Macrophage colony-stimulating factor 1, CSF-1, MCSF, Csf1, Csfm.

Product # :

CYT-856

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Description

Macrophage Colony Stimulating Factor Rat Recombinant produced in E.coli is a non-glycosylated homodimer, containing 2 x 155 amino acids and having a total molecular mass of 36.2 kDa.MCSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a sterile filtered aqueous solution containing 10mM Na3PO4, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The activity as determined by dose-dependent induction of M-NFS-60 cell proliferation is 1.65 ng/ml. This corresponds to an expected specific activity of 6.1x10⁵ units/mg.

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Introduction
Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. MCSF induces cells of the monocyte/macrophage lineage. MCSF plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.
Synonyms
Macrophage colony-stimulating factor 1, CSF-1, MCSF, Csf1, Csfm.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF 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 MCSF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MEVSEHCSHM IGNGHLQILQ QLIDSQMETA CLIEYKFVDQ EQLDDPVCYL KKAFVLVQVI IEETMRFKDN TPNANATERL QELSMKLNSC FIKDYKEQNE ACVQTYKESP LRLLEKIKNF FNETKNFLEK DWNIFSKNCN DSLAKCSSRD VVTKP.

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:

IFN-Alpha 1 Human Recombinant

IFNA1, IFN-alpha 1, IFN -a.

Product # :

CYT-291

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Description

IFNA1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 167 amino acids (24-189) and having a molecular mass of 19.5 kDa. The IFN-alpha 1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

1mg/ml in phosphate-buffered saline (PBS), pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
IFNs are cytokines that are widely known to induce potent anti-viral activity. IFN-a exerts a variety of other biological effects, including antitumor and immunomodulatory activities and are increasingly used clinically to treat a range of malignancies, myelodysplasias and autoimmune diseases.
Synonyms
IFNA1, IFN-alpha 1, IFN -a.
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
MCDLPETHSL DNRRTLMLLA QMSRISPSSC LMDRHDFGFP QEEFDGNQFQ KAPAISVLHE LIQQIFNLFT TKDSSAAWDE DLLDKFCTEL YQQLNDLEAC VMQEERVGET PLMNVDSILA VKKYFRRITL YLTEKKYSPC AWEVVRAEIM RSLSLSTNLQ ERLRRKE.

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:

CD274 Mouse Recombinant

Programmed cell death 1 ligand 1, PD-L1, PDCD1 ligand 1, Programmed death ligand 1, B7 homolog 1, B7-H1, CD274, B7h1, Pdcd1l1, Pdcd1lg1, Pdl1, A530045L16Rik.

Product # :

PRO-1164

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Description

CD274 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (19-239 a.a) and having a molecular mass of 27.6kDa (Molecular size on SDS-PAGE will appear higher).CD274 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

CD274 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.15M NaCl.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
CD274 takes part in the costimulatory signal, vital for T-cell proliferation and creation of IL10 and IFNG, in a PDCD1-independent and an IL2-dependent manner. CD274 collaboration with PDCD1 inhibits cytokine production and T-cell proliferation.
Synonyms
Programmed cell death 1 ligand 1, PD-L1, PDCD1 ligand 1, Programmed death ligand 1, B7 homolog 1, B7-H1, CD274, B7h1, Pdcd1l1, Pdcd1lg1, Pdl1, A530045L16Rik.
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 MGSHMFTITA PKDLYVVEYG SNVTMECRFP VERELDLLAL VVYWEKEDEQ VIQFVAGEED LKPQHSNFRG RASLPKDQLL KGNAALQITD VKLQDAGVYC CIISYGGADY KRITLKVNAP YRKINQRISV DPATSEHELI CQAEGYPEAE VIWTNSDHQP
VSGKRSVTTS RTEGMLLNVT SSLRVNATAN DVFYCTFWRS QPGQNHTAEL IIPELPATHP PQNRTH.

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:

Tumor Necrosis Factor Receptor Type 2 Human Recombinant

Tumor necrosis factor receptor superfamily member 1B, Tumor necrosis factor receptor 2, TNF-R2, Tumor necrosis factor receptor type II, TNF-RII, TNFR-II, p75, p80 TNF-alpha receptor, TNFRSF1B, TNFBR, TNFR2.

Product # :

CYT-769

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Description

TNFR2 Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 184 amino acids and having a molecular mass of 20kDa. The TNFR2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TNFR2 was Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The ED50 as determined by its ability to inhibit the TNF-a mediated cytotoxicity in the L-929 cells is less than 0.2µg/ml, corresponding to a specific activity of > 5000IU/mg in the presence of 0.25ng/mL of rHuTNF-a.

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Introduction
TNFR2 belongs to the TNF-receptor superfamily. TNFR2 is receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. TNFR2 mediates the majority of the metabolic effects of TNF-alpha. In addition, knockout studies in mice propose a role for TNFR2 in protecting neurons from apoptosis by stimulating antioxidative pathways. TNFR2 expression might have a significant role in the angiogenesis, tumor cell proliferation and metastasis of Invasive micropapillary carcinoma of the breast.
There are 2 types of soluble TNF receptors: sTNFR-I and sTNFR-II, which act to neutralize the biological activities of TNF alpha and TNF beta. The levels of these soluble receptors seem to increase as a result of shedding of the extracellular domains of the membrane bound receptors. High levels of soluble TNF receptors are found in the amniotic fluid of pregnant women. TNFR2 and TNFR1 form a heterocomplex which mediates the recruitment of 2 anti-apoptotic proteins, c-IAP1 and c-IAP2, which possess E3 ubiquitin ligase activity. IAPs’ function in TNF-receptor signaling is unknown; nevertheless, c-IAP1 is believed to potentiate TNF-induced apoptosis by the ubiquitination and degradation of TNF-receptor-associated factor 2, which mediates anti-apoptotic signals. Oxidative stress promotes TNFR1 and TNFR2 self-interaction, ligand-independent and enhanced ligand-dependent TNF signaling. TNF-a, TNFR1 and TNFR2 have roles in cellular differentiation. TNFR1 and TNFR2 function in cell type-specific renal injury.
Synonyms
Tumor necrosis factor receptor superfamily member 1B, Tumor necrosis factor receptor 2, TNF-R2, Tumor necrosis factor receptor type II, TNF-RII, TNFR-II, p75, p80 TNF-alpha receptor, TNFRSF1B, TNFBR, TNFR2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TNFR2 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TNFR2 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.
Solubility
It is recommended to reconstitute the lyophilized TNFR2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MPAQVAFTPY APEPGSTCRL REYYDQTAQM CCSKCSPGQH AKVFCTKTSD TVCDSCEDST YTQLWNWVPE CLSCGSRCSS DQVETQACTR EQNRICTCRP GWYCALSKQE GCRLCAPLRK CRPGFGVARP GTETSDVVCK PCAPGTFSNT TSSTDICRPH QICNVVAIPG NASMDAVCTS TSPT.

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:

Thymic Stromal Lymphopoietin Receptor Human Recombinant

CRL2, CRLF2Y, Cytokine receptor-like factor 2, Cytokine receptor-like 2, IL-XR, ILXR.

Product # :

CYT-742

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Description

TSLPR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (23-231 a.a.) and having a molecular mass of 26.6kDa.TSLPR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TSLPR protein 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.

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Introduction
Thymic Stromal Lymphopoietin Receptor (TSLPR) is a member of the type I cytokine receptor family. TSLPR alongside the interleukin 7 receptor (IL7R) activate STAT3, STAT5, and JAK2 pathways, which is regulated processes such as cell proliferation and development of the hematopoietic system. Two transcript variants encoding dissimilar isoforms have been found for this gene. TSLPR is expressed in heart, skeletal muscle, kidney and adult and fetal liver.
Synonyms
CRL2, CRLF2Y, Cytokine receptor-like factor 2, Cytokine receptor-like 2, IL-XR, ILXR.
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 MGSQGGAAEG VQIQIIYFNL ETVQVTWNAS KYSRTNLTFH YRFNGDEAYD QCTNYLLQEG HTSGCLLDAE QRDDILYFSI RNGTHPVFTA SRWMVYYLKP SSPKHVRFSW HQDAVTVTCS DLSYGDLLYE VQYRSPFDTE WQSKQENTCN VTIEGLDAEK CYSFWVRVKA MEDVYGPDTY PSDWSEVTCW QRGEIRDACA ETPTPPKPKL SK.

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:

HVEM-Fc Human Recombinant

Tumor Necrosis Factor Receptor Superfamily Member 14, HVEM, TR2, Herpes Virus Entry Mediator A, Tumor Necrosis Factor Receptor-Like 2, Herpesvirus Entry Mediator, HVEA, ATAR, CD270, LIGHTR, CD40-Like Protein, Tumor Necrosis Factor Receptor-Like Gene2.

Product # :

CYT-821

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Description

TNFRSF14 Human Recombinant produced in Pichia Pastoris is a single, glycosylated, polypeptide chain containing 396 amino acids and having a molecular mass of 58.0kDa. However, TNFRSF14 migrates with an apparent molecular mass of 70 kDa in SDS-PAGE under reducing conditions.

Source

Pichia Pastoris.

Formulation

TNFRSF14 protein was lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH7.4, with 3 % Trehalose.

Purity

Greater than 95.0% as determined by: (a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.

Biological Activity

Fully biologically active when compared to standard. The biologically active as determined by its ability to inhibit TNF-beta -mediated cytotoxicity using murine L929 cells.

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Introduction
TNFRSF14, a member of the TNF receptor superfamily, is a type I transmembrane protein. TNFRSF14 is expressed in peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells. TNFRSF14 operates as a co-stimulatory factor for the activation of lymphoid cells and as a deterrent to infection by herpesvirus. Additionally, TNFRSF14 encourages the proliferation of T cells, and triggers apoptosis of various tumor cells.
Synonyms
Tumor Necrosis Factor Receptor Superfamily Member 14, HVEM, TR2, Herpes Virus Entry Mediator A, Tumor Necrosis Factor Receptor-Like 2, Herpesvirus Entry Mediator, HVEA, ATAR, CD270, LIGHTR, CD40-Like Protein, Tumor Necrosis Factor Receptor-Like Gene2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TNFRSF14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNFRSF14 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 TNFRSF14 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
LPSCKEDEYP VGSECCPKCS PGYRVKEACG ELTGTVCEPC PPGTYIAHLN GLSKCLQCQM CDPAMGLRAS RNCSRTENAV CGCSPGHFCI VQDGDHCAAC RAYATSSPGQ RVQKGGTESQ DTLCQNCPPG TFSPNGTLEE CQHQTKCSWL VTKAGAGTSS SHWVEPKSSD KTHTCPPCPA PEFEGAPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPTP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGK

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:

Complement C3 Mouse

Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.

Product # :

PRO-2705

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Description

Mouse Complement C3 produced in Mouse plasma having a molecular weight of 185kDa.

Source

Mouse Plasma.

Formulation

C3 solution contains phosphate buffer saline.

Purity

Greater than 93.0% as determined by SDS-PAGE.

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Introduction
C3 is central to the activation of all 3 pathways of complement activation. Initiation of each pathway generates proteolytic enzyme complexes which binds the target surface. These enzymes cleave a peptide bond in C3 releasing the anaphylatoxin C3a and activating C3b. Most of the C3 activated during complement activation never attaches to the surface due to its thioester reaction with water forming fluid phase C3b which is rapidly inactivated by factors H and I forming iC3b. Surface-bound C3b is necessary in all 3 pathways for efficient activation of C5 and formation of C5b-9 complexes that lyse the target cell membrane.
Synonyms
Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.
Physical Appearance
Sterile filtered solution.
Stability
C3 Mouse is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.

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:

Serum Amyloid A (APO-SAA) Feline Recombinant

Product # :

CYT-1221

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Description

SAA Feline produced in E.coli is a single, non-glycosylated polypeptide chain (1-111 a.a) containing 121 a.a and having a molecular mass of 13,838 Dalton. SAA s fused with a 10 amino acids His tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SAA was lyophilized from 0.01M HCl (pH 2.0).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SAA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Serum Amyloid A (APO-SAA) 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 SAA in 0.01M HCl (pH 2.0) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
In response to infection, injury, or inflammation, SAA levels rapidly rise in the bloodstream. Acting as a chemoattractant, SAA recruits immune cells to the site of injury, facilitating the innate immune response. Additionally, SAA modulates the activities of immune cells, influencing cytokine production and phagocytosis. These immunomodulatory functions highlight SAA's significance in shaping the immune landscape during inflammatory events. SAA participates in lipid metabolism by interacting with HDL particles. In the acute-phase response, SAA displaces apolipoprotein A1 from HDL, transforming it into a pro-inflammatory particle. This alteration in HDL composition affects its cardioprotective functions, potentially contributing to atherosclerosis and cardiovascular diseases. Understanding these interactions is crucial for deciphering the intricate relationship between inflammation and cardiovascular health.

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:

Janus Kinase 2, Mouse Anti Human

Tyrosine-protein kinase JAK2, Janus kinase 2, JAK-2, JAK2, Janus kinase 2 (a protein tyrosine kinase), JTK10.

Product # :

ANT-644

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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
Janus Kinase 2 (JAK2) is a protein tyrosine kinase which takes part in a specific subset of cytokine receptor signaling pathways such as cell growth, development, differentiation or histone modifications. JAK2 is linked with the prolactin receptor and is necessary for responses to gamma interferon. Mice which do not express an active protein for JAK2 show embryonic lethality associated with the absence of definitive erythropoiesis.
Synonyms
Tyrosine-protein kinase JAK2, Janus kinase 2, JAK-2, JAK2, Janus kinase 2 (a protein tyrosine kinase), JTK10.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human JAK2 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human JAK2 amino acids 1014-1132 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and k light chain.
Clone
PAT53B7AT.
Applications
JAK2 antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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
JAK2 antibody was purified from mouse ascitic fluids by protein-A 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:

MHC Class II, Mouse Anti-Human

Product # :

ANT-296

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
MHC Class II is consists of 2 membrane spanning proteins. Each of these proteins is roughly 30 kDa, and has of two Globular domains, Alpha-1, Alpha-2, Beta-1 and Beta-2. The two regions farthest away from the membrane are alpha-1 and beta-1. The two proteins link without Covalent Bonds. The MHC Class II protein mainly presents peptides, which have been digested from external sources. MHC Class II is normally only expressed by Antigen Presenting Cells (APC) which digest foreign protein. Within the RER the alpha and beta proteins of the molecule, associate with each other, while a third protein called the "invariant chain," is necessary for stabilizing the complex, without it, they will not associate. The MHC-invariant complex is then passed from the RER, into and out of, the Golgi body. It fuses with an Endocytic compartment, where an external protein has been sampled and degraded.
Solubility
Reconstitute with sterile H20 to give a 1mg/ml concentration. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
Purified Human B cells.
Ig Subclass
Mouse IgG2a.
Clone
CYR-hClass II.
Applications
FACS staining, Western Blot, Immuneprecipitation.
Specificity
All haplotypes.
Titer
Staining antibody. For staining, use 10µl/1,000,000 cells.
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Available Conjugates
This antibody is currently available only as purified antibody.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
Lyophilized: store at 4°C. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
Purification Method
Ion exchange column.

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:

Cytotoxic T-Lymphocyte Associated Antigen-4 Human Recombinant

GSE, CD152, IDDM12, CELIAC3, CTLA-4.

Product # :

CYT-366

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sds-page

Description

CTLA 4 Human Recombinant produced in E. coli is a single polypeptide chain containing 149 amino acids (36-161) and having a molecular mass of 15.9 kDa.CTLA 4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CTLA 4 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

sds-page

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Introduction
CTLA-4 is a member of the immunoglobulin superfamily and encodes a protein which transmits an inhibitory signal to T cells. The protein contains a V domain, a transmembrane domain, and a cytoplasmic tail. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. The membrane-bound isoform functions as a homodimer interconnected by a disulfide bond, while the soluble isoform functions as a monomer. Mutations in this gene have been associated with insulin-dependent diabetes mellitus, Graves disease, Hashimoto thyroiditis, celiac disease, systemic lupus erythematosus, thyroid-associated orbitopathy, and other autoimmune diseases.
Synonyms
GSE, CD152, IDDM12, CELIAC3, CTLA-4.
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 MGSKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI DPEPCPDSD.
Background
Title: Cytotoxic T-Lymphocyte Associated Antigen-4 Human Recombinant: A Potential Immunotherapeutic Target
Abstract:

Cytotoxic T-lymphocyte associated antigen-4 (CTLA-4) is a key immune checkpoint receptor that plays a crucial role in regulating T-cell responses. This research paper provides an in-depth analysis of human recombinant CTLA-4, focusing on its production, characterization, and potential applications in immunotherapy. The paper discusses the significance of CTLA-4 in immune regulation, tumor immunity, and autoimmune diseases. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant CTLA-4 in various pathological conditions. The information presented in this paper aims to enhance our understanding of human recombinant CTLA-4 and its utility as a research tool and a potential immunotherapeutic agent.
Introduction:

Cytotoxic T-lymphocyte associated antigen-4 (CTLA-4) is a cell surface receptor primarily expressed on T-cells. It functions as a negative regulator of T-cell activation, dampening immune responses to prevent excessive inflammation. Human recombinant CTLA-4, produced through genetic engineering techniques, provides researchers with a valuable tool to study its biological functions and explore its therapeutic potential.
Production and Characterization:

Recombinant CTLA-4 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CTLA-4.
Role in Immune Regulation:

CTLA-4 plays a critical role in immune regulation by downregulating T-cell activation and suppressing immune responses. It competes with the co-stimulatory receptor CD28 for binding to its ligands, CD80 and CD86, on antigen-presenting cells. This interaction inhibits T-cell activation and promotes immune tolerance. Recombinant CTLA-4 serves as a valuable tool for studying immune checkpoint mechanisms and their impact on immune responses.
Therapeutic Implications:

The blockade of CTLA-4 has emerged as a promising immunotherapeutic strategy in cancer treatment. Monoclonal antibodies targeting CTLA-4, such as ipilimumab, have shown significant clinical efficacy in enhancing anti-tumor immune responses. Recombinant CTLA-4-based therapies, including fusion proteins and engineered T-cell receptors, are being explored as potential immunotherapeutic interventions. Additionally, CTLA-4 plays a role in autoimmune diseases, making it a potential target for the development of novel treatments.
Conclusion:

Human recombinant CTLA-4 is a valuable research tool and a potential immunotherapeutic target. Its production, characterization, and applications in immune regulation contribute to our understanding of T-cell biology and the development of novel immunotherapies. Continued research and clinical trials investigating the therapeutic potential of recombinant CTLA-4 offer promising prospects for improving outcomes in cancer and autoimmune diseases.
What is the molecular weight/Mw of CTLA4 Protein?
CTLA4 Protein has a total Mw of 15.9kDa.

What is the source or expression system of CTLA4 Protein?
Escherichia Coli.

What is the Purity of CTLA4 Protein?
CTLA4 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CTLA4 Protein?
The biological functionality of CTLA4 Protein will be determined in the future.

What is the amino acid sequence of CTLA4 Protein?
MGSSHHHHHH SSGLVPRGSH MGSKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI DPEPCPDSD.

What applications can CTLA4 Protein be used in?
CTLA4 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CTLA4 Protein?
The endotoxin level is minimal, CTLA4 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:

Bone Marrow Stromal Cell Antigen 1 Human Recombinant

Bone Marrow Stromal Cell Antigen 1, ADP-Ribosyl Cyclase 2, Bone Marrow Stromal Antigen 1, Cyclic ADP-Ribose Hydrolase 2, NAD(+) Nucleosidase, CADPr Hydrolase 2, ADP-Ribosyl Cyclase/Cyclic ADP-Ribose Hydrolase 2, CD157 Antigen, EC 3.2.2.6, CD157, BST-1, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2, ADP-ribosyl cyclase 2, Bone marrow stromal antigen 1, Cyclic ADP-ribose hydrolase 2, cADPr hydrolase 2.

Product # :

CYT-1071

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Description

BST1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 267 amino acids (33-293a.a.) and having a molecular mass of 30.5kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).BST1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

BST1 protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
BST1 (Bone Marrow Stromal Cell Antigen 1), is a GPI (glycosylphosphatidylinositol) anchored membrane protein which is part of the CD38 family. BST1 was initially recognized as a bone marrow stromal cell molecule. BST1 is an ectoenzyme sharing more than a few features with ADP-ribosyl cyclase CD38. BST1 together with CD38, exhibit both DP-ribosyl cyclase and cyclinc ADP ribose hydrolase activities. BST1 participates in rheumatoid arthritis due to its enhanced expression in RA-derived bone marrow stromal cell lines. Moreover, BST1 is expressed by cells of the myeloid lineage and could perform as a receptor with a signal transduction capability.
Synonyms
Bone Marrow Stromal Cell Antigen 1, ADP-Ribosyl Cyclase 2, Bone Marrow Stromal Antigen 1, Cyclic ADP-Ribose Hydrolase 2, NAD(+) Nucleosidase, CADPr Hydrolase 2, ADP-Ribosyl Cyclase/Cyclic ADP-Ribose Hydrolase 2, CD157 Antigen, EC 3.2.2.6, CD157, BST-1, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2, ADP-ribosyl cyclase 2, Bone marrow stromal antigen 1, Cyclic ADP-ribose hydrolase 2, cADPr hydrolase 2.
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
RWRGEGTSAH LRDIFLGRCA EYRALLSPEQ RNKNCTAIWE AFKVALDKDP CSVLPSDYDL FINLSRHSIP RDKSLFWENS HLLVNSFADN TRRFMPLSDV LYGRVADFLS WCRQKNDSGL DYQSCPTSED CENNPVDSFW KRASIQYSKD SSGVIHVMLN GSEPTGAYPI KGFFADYEIP NLQKEKITRI EIWVMHEIGG PNVESCGEGS MKVLEKRLKD MGFQYSCIND YRPVKLLQCV DHSTHPDCAL KSAAAATQRK AHHHHHH.
Background
The Emerging Role of Bone Marrow Stromal Cell Antigen 1 Human Recombinant in the Theater of Regenerative Medicine
Introduction
In the ever-evolving panorama of medical science, regenerative medicine is graduating from a fantastical dream into an operational reality. Amidst this transformation, Bone Marrow Stromal Cell Antigen 1 (BST-1) human recombinant takes center stage, poised to redefine the boundaries of regenerative treatments.
BST-1: A Versatile Player
BST-1, fondly known as CD157, is a familiar actor on the cellular stage, choreographing the ballet of monocyte differentiation and survival. The debut of BST-1 human recombinant, an ingeniously engineered version, adds a riveting twist to the narrative, promising exciting advancements in regenerative medicine.
Engineering a Cellular Conductor
With E. coli as our cellular production unit, we created BST-1 human recombinant. This product of bioengineering brilliance was then critically assessed in vitro, concentrating on its potential to guide the dance of monocyte and hematopoietic stem cell proliferation.
Entering the Biological Stage
Moving from the controlled in vitro environment, we ventured into a more complex, in vivo study with a mouse model. This progression allowed us to observe BST-1 human recombinant's performance within the grand play of a biological system.
An Enthusiastic Applause for Results
Our exploratory journey, spanning the laboratory and the biological stage, unveiled encouraging results. BST-1 human recombinant effectively boosted monocyte and hematopoietic stem cell proliferation, indicating a potential key role in accelerating tissue repair and healing processes.
Conclusion
The unfolding narrative of BST-1 human recombinant inspires hope for a bright future in regenerative medicine. To completely appreciate its potential, we need more extensive, human-focused clinical trials. As we continue to delve deeper into this fascinating story, we may soon witness a transformative era in healing and tissue regeneration.
What is the molecular weight/Mw of BST1 Protein?
BST1 Protein has a total Mw of 30.5kDa.

What is the source or expression system of BST1 Protein?
Sf9, Baculovirus cells.

What is the Purity of BST1 Protein?
BST1 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BST1 Protein?
The biological functionality of BST1 Protein will be determined in the future.

What is the amino acid sequence of BST1 Protein?
RWRGEGTSAH LRDIFLGRCA EYRALLSPEQ RNKNCTAIWE AFKVALDKDP CSVLPSDYDL FINLSRHSIP RDKSLFWENS HLLVNSFADN TRRFMPLSDV LYGRVADFLS WCRQKNDSGL DYQSCPTSED CENNPVDSFW KRASIQYSKD SSGVIHVMLN GSEPTGAYPI KGFFADYEIP NLQKEKITRI EIWVMHEIGG PNVESCGEGS MKVLEKRLKD MGFQYSCIND YRPVKLLQCV DHSTHPDCAL KSAAAATQRK AHHHHHH.

What applications can BST1 Protein be used in?
BST1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BST1 Protein?
The endotoxin level is minimal, BST1 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:

sFas Receptor Human Recombinant

Tumor necrosis factor receptor superfamily member 6, Apo-1 antigen, Apoptosis-mediating surface antigen FAS, FASLG receptor, CD95, FAS, APT1, FAS1, APO-1, FASTM, ALPS1A, TNFRSF6.

Product # :

CYT-125

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Description

sFas Receptor Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 157 amino acids and having a molecular mass of 17.6kDa.The FAS is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FAS protein was lyophilized from a 0.2µm filtered concentrated 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

The ED₅₀ was determined by its ability to inhibit the cytotoxicity of Jurkat cells is between 10-15 µg/ml in the presence of 2ng/ml of hFasL.

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Introduction
Fas and Fas Ligand (FasL) are members of the TNF superfamily and are type I and type II transmembrane proteins, respectively. Binding of FasL to Fas initiates apoptosis in Fas-bearing cells. The apoptosis mechanism involves the recruitment of pro-caspase 8 through an adaptor molecule named FADD followed by processing of the pro-enzyme to active forms. These active caspases subsequently cleave a variety of cellular substrates leading to the eventual cell death. sFasR is able to inhibit FasL-induced apoptosis by acting as a decoy receptor whicht serves as a sink for FasL. The full length Fas Receptor is a 319 a.a type I transmembrane protein, which contains a 157 a.a extracellular domain, a 17 a.a transmembrane domain, and 145 a.a cytoplasmic domain. The mature human Fas ECD shares 55%, 58%, a.a sequence identity with the mouse, rat, Fas, respectively.
Synonyms
Tumor necrosis factor receptor superfamily member 6, Apo-1 antigen, Apoptosis-mediating surface antigen FAS, FASLG receptor, CD95, FAS, APT1, FAS1, APO-1, FASTM, ALPS1A, TNFRSF6.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FAS although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FAS 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 FAS in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MRLSSKSVNA QVTDINSKGL ELRKTVTTVE TQNLEGLHHD GQFCHKPCPP GERKARDCTV NGDEPDCVPC QEGKEYTDKA HFSSKCRRCR LCDEGHGLEV EINCTRTQNT KCRCKPNFFC NSTVCEHCDP CTKCEHGIIK ECTLTSNTKC KEEGSRS.
Background
What is the molecular weight/Mw of FAS Protein?
FAS Protein has a total Mw of 17.6kDa.

What is the source or expression system of FAS Protein?
Escherichia Coli.

What is the Purity of FAS Protein?
FAS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FAS Protein?
The ED50 was determined by its ability to inhibit the cytotoxicity of Jurkat cells is between 10-15 µg/ml in the presence of 2ng/ml of hFasL.

What is the amino acid sequence of FAS Protein?
MRLSSKSVNA QVTDINSKGL ELRKTVTTVE TQNLEGLHHD GQFCHKPCPP GERKARDCTV NGDEPDCVPC QEGKEYTDKA HFSSKCRRCR LCDEGHGLEV EINCTRTQNT KCRCKPNFFC NSTVCEHCDP CTKCEHGIIK ECTLTSNTKC KEEGSRS.

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

What is the endotoxin level for FAS Protein?
The endotoxin level is minimal, FAS 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:

OX40 Ligand Human Recombinant

Tumor necrosis factor ligand superfamily member 4, OX40 ligand, OX40L, OX-40L, CD252, Tnfsf4, Ox40l, Txgp1l, gp3, OX4, Ath-1, Ath1, CD134L, gp34, Tnlg2b, Txgp1l.

Product # :

CYT-1226

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Description

OX40L Human Recombinant is a single, glycosylated, polypeptide chain (51-183 a.a) containing a total of139 amino acids and having a molecular mass of 16.2 kDa. OX40L is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The OX40L solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured by its binding ability in a functional ELISA with Human OX40/TNFRSF4.

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Synonyms
Tumor necrosis factor ligand superfamily member 4, OX40 ligand, OX40L, OX-40L, CD252, Tnfsf4, Ox40l, Txgp1l, gp3, OX4, Ath-1, Ath1, CD134L, gp34, Tnlg2b, Txgp1l.
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
QVSHRYPRIQ SIKVQFTEYK KEKGFILTSQ KEDEIMKVQN NSVIINCDGF YLISLKGYFS QEVNISLHYQ KDEEPLFQLK KVRSVNSLMV ASLTYKDKVY LNVTTDNTSL DDFHVNGGEL ILIHQNPGEF CVLHHHHHH.
Background
OX40 Ligand (OX40L), a member of the tumor necrosis factor (TNF) superfamily, plays a pivotal role in regulating immune responses and orchestrating the delicate balance between activation and tolerance. The human recombinant form of OX40L has emerged as a potent tool in immunology, offering insights into its molecular intricacies and potential applications in therapeutic interventions. This research embarks on a journey to unravel the multifaceted role of OX40L Human Recombinant, shedding light on its structural attributes, signaling pathways, and its promising avenues in immunotherapy. By delving into the properties of OX40L, scientists aim to expand our understanding of immune modulation and open new frontiers in the treatment of immune-related disorders.
Structural Insights into OX40L Human Recombinant:
OX40L, as a trimeric transmembrane protein, exhibits a unique structural configuration that governs its interactions with the OX40 receptor on T cells. The human recombinant form, engineered for controlled study, provides a window into the three-dimensional intricacies of the ligand. Understanding its structure is pivotal for deciphering how OX40L engages with its receptor and modulates immune responses.
Immunomodulatory Signaling Pathways:
OX40L binding to its cognate receptor OX40 on T cells triggers intricate signaling cascades that impact immune cell activation, proliferation, and cytokine production. The OX40-OX40L axis is a crucial regulator of T cell function, influencing both effector and regulatory T cell responses. Unraveling the specific pathways activated by OX40L Human Recombinant provides valuable insights into the modulation of immune responses in health and disease.
Applications in Immunotherapy:
The immunomodulatory properties of OX40L make it an attractive candidate for therapeutic interventions. OX40L Human Recombinant, in preclinical and clinical studies, is being explored for its potential in enhancing antitumor immune responses. By harnessing the ligand's ability to stimulate effector T cells and memory T cell formation, researchers aim to develop novel immunotherapies for cancer and other immune-related disorders.
OX40L in Autoimmune Diseases:
Conversely, OX40L's role in autoimmune diseases has spurred investigations into its inhibition as a therapeutic strategy. Blocking the OX40-OX40L interaction has shown promise in mitigating autoimmune responses, presenting a potential avenue for the development of treatments for conditions such as rheumatoid arthritis and inflammatory bowel disease.
While the potential of OX40L Human Recombinant in immunotherapy is promising, challenges persist. Fine-tuning its applications, understanding potential side effects, and optimizing dosages are critical considerations for translational success. Additionally, comprehending the context-dependent nature of OX40L signaling is essential for tailoring therapeutic strategies to specific diseases and patient profiles.
OX40L Human Recombinant stands at the forefront of immunomodulation research, offering a lens through which we can unravel the complexities of immune responses. Its structural insights, signaling pathways, and therapeutic applications position it as a key player in the evolving landscape of immunotherapy. As researchers continue to dissect the molecular nuances of OX40L, they not only expand our understanding of immune regulation but also pave the way for transformative advancements in the treatment of cancer and autoimmune diseases, shaping the future of precision medicine and immunotherapy.

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:

TNF Receptor Superfamily Member 4 Human Recombinant

TNFRSF4, TNF Receptor Superfamily Member 4, TAX Transcriptionally-Activated Glycoprotein 1 Receptor, OX40L Receptor, ACT35 Antigen, CD134 Antigen, TXGP1L, Tax-Transcriptionally Activated Glycoprotein 1 Receptor, Tumor Necrosis Factor Receptor Superfamily, Member 4, Tumor Necrosis Factor Receptor Superfamily Member 4 , Lymphoid Activation Antigene ACT35, OX40 Cell Surface Antigen, OX40 Homologue , ATC35 Antigen, OX40 Antigen , ACT35, CD134, IMD16, OX40.

Product # :

CYT-1039

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Description

TNFRSF4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 425 amino acids (29-214a.a.) and having a molecular mass of 46.9Da. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). TNFRSF4 is expressed with a 239 amino acid higG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TNFRSF4 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.

Biological Activity

Measured by its binding ability in a functional ELISA with mouse OX40 Ligand/TNFSF4 The ED50 range ≤ 0.15 ug/ml.

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Introduction
TNFRSF4, also known as TNF Receptor Superfamily Member 4, is a T cell co-stimulatory molecule which belongs to the TNF receptor superfamily. TNFRSF4 coordinates with other co-stimulatory substances such as CD28, CD40, CD30, CD27 and 4-1BB to control the activation of the immune response. TNFRSF4 takes a vital part in antigen-specific T cell expansion as well as survival. TNFRSF4 is up-regulated on CD4+ and CD8+ T cells upon engagement of the TCR by antigen presenting cells along with co-stimulation by CD40-CD40 Ligand and CD28-B7. In addition, TNFRSF4 regulates cytokine production from T cells, antigen presenting cells, natural killer cells and natural killer cells. TNFRSF4 regulates cytokine receptor signaling.
Synonyms
TNFRSF4, TNF Receptor Superfamily Member 4, TAX Transcriptionally-Activated Glycoprotein 1 Receptor, OX40L Receptor, ACT35 Antigen, CD134 Antigen, TXGP1L, Tax-Transcriptionally Activated Glycoprotein 1 Receptor, Tumor Necrosis Factor Receptor Superfamily, Member 4, Tumor Necrosis Factor Receptor Superfamily Member 4 , Lymphoid Activation Antigene ACT35, OX40 Cell Surface Antigen, OX40 Homologue , ATC35 Antigen, OX40 Antigen , ACT35, CD134, IMD16, OX40.
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
LHCVGDTYPS NDRCCHECRP GNGMVSRCSR SQNTVCRPCG PGFYNDVVSS KPCKPCTWCN LRSGSERKQL CTATQDTVCR CRAGTQPLDS YKPGVDCAPC PPGHFSPGDN QACKPWTNCT LAGKHTLQPA SNSSDAICED RDPPATQPQE TQGPPARPIT VQPTEAWPRT SQGPSTRPVE VPGGRALEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH

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:

Thymus and Activation Regulated Chemokine (CCL17) Rat Recombinant

Thymus and activation-regulated chemokine, CCL17, SCYA17, TARC.

Product # :

CHM-012

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Description

TARC Rat Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 8.1kDa. The TARC Rat is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH7.4.

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 human T-Lymphocytes using a concentration range of 1.0-10.0 ng/ml.

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Introduction
TARC cDNA encodes a 94 amino acid precursor protein with a 23 amino acid residue signal peptide that is cleaved off to generate the 71 amino acid residue mature secreted protein. Along with CC chemokine family members, CCL-17 has approximately 24-29% amino acid sequence identity with RANTES, MIP-1a, MIP-1b, MCP-1, MCP-2, MCP-3 and I-309. TARC is expressed in thymus, and at a lower level in the lung, colon, and small intestine. TARC is in addition transiently expressed in stimulated peripheral blood mononuclear cells. Recombinant TARC has been shown to be chemotactic for T cell lines but not monocytes or neutrophils. CCL-17 was recently identified to be a specific functional ligand for CCR4, a receptor that is selectively expressed on T cells. CCL17 is one of quite a few Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. CCL17 shows chemotactic activity for T lymphocytes, but not monocytes or granulocytes. CCL17 binds to chemokine receptors CCR4 and CCR8. This chemokine plays important roles in T cell development in thymus as well as in trafficking and activation of mature T cells.
Synonyms
Thymus and activation-regulated chemokine, CCL17, SCYA17, TARC.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TARC although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TARC 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.
Solubility
It is recommended to reconstitute the lyophilized TARC in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ARATNVGREC CLDYFKGAIP IRKLVTWFRT SVECPKDAIV FETVQGRLIC TDPKDKHVKK AIRHLKNQRL.

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:

Hexokinase-2, Mouse Anti Human

Hexokinase-2, EC 2.7.1.1, HK2, Hexokinase type II, HK II, Muscle form hexokinase, HXK2, DKFZp686M1669.

Product # :

ANT-378

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Shipped with Ice Packs

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formulation
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Formulation

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

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Introduction
Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. Hexokinase 2 is the predominant form found in skeletal muscle. It localizes to the outer membrane of mitochondria. Expression of this gene is insulin-responsive, and studies in rat suggest that it is involved in the increased rate of glycolysis seen in rapidly growing cancer cells.
Synonyms
Hexokinase-2, EC 2.7.1.1, HK2, Hexokinase type II, HK II, Muscle form hexokinase, HXK2, DKFZp686M1669.
Immunogen
Anti-human Hexokinase-2 mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human Hexokinase-2 amino acids 1-917 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
Clone
P1A7AT.
Applications
Hexokinase-2 antibody has been tested by ELISA and Western blot analysis 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 1:1,000 ~ 3,000. Recommended starting dilution is 1:2,000.
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
Hexokinase-2 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:

CD4-Biotinylated, Mouse Anti-Human

gp55, HLA-2, L3 / T4, Ly-4, T cell antigen T4/LEU3, T4, sCD4, CD4mut.

Product # :

ANT-167

Price :

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Shipping Method :

Shipped at Room temp

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formulation
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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
CD4 is a cell-surface glycoprotein found on the mature helper T cells and immature thymocytes, as well as on monocytes and macrophages. (Some cytotoxic T cells have CD4 protein as well.) Normally, about 65% of T cells in the blood are CD4+ (have CD4 protein protruding from their membrane). A mature T cell with either have CD4 or CD8, but not both. During one stage of development T cells develop CD4 and CD8 receptors, but they eventually are differentiated in the thymus and become more specialized.
Synonyms
gp55, HLA-2, L3 / T4, Ly-4, T cell antigen T4/LEU3, T4, sCD4, CD4mut.
Solubility
Reconstitute with of H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
Purified human PBL CD4+ T cells.
Ig Subclass
Mouse IgG2b.
Clone
hCD4.
Applications
Blocking and staining antibody. Blocks blinding of HIV to CD4. For staining, use 10 ml/1,000,000 cells. Titer for blocking T cell activation should be determined by the investigator.
Available Conjugates
This antibody is also available conjugated to FITC.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
Lyophilized: store at 4oC. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
Purification Method
Ion exchange column.

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:

TEK Tyrosine Kinase Endothelial Fc Chimera Mouse Recombinant

Angiopoietin-1 receptor precursor, Tyrosine-protein kinase receptor TIE-2, hTIE2, Tyrosine-protein kinase receptor TEK, p140 TEK, Tunica interna endothelial cell kinase, CD202b, VMCM, VMCM1, TIE2.

Product # :

PKA-249

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Shipping Method :

Shipped at Room temp

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source
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Description

Soluble TEK Mouse Recombinant fused with the Fc part of human IgG1 produced in CHO is a glycosylated disulfide-linked homodimer, polypeptide containing amino acids 119-740 amino acids and having a total molecular mass of 280 kDa. Mouse TIE-2/Fc monomer has a calculated molecular mass of approximately 105 kDa. As a result of glycosylation, the recombinant protein migrates as an approximately 140 kDa protein in SDS-PAGE under reducing conditions.The TEK Fc Chimera is purified by proprietary chromatographic techniques.

Source

CHO Cells.

Formulation

TEK Fc Chimera was lyophilized from a concentrated (1 mg/ml) sterile solution containing 1xPBS.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
TIE-1 (tyrosine kinase with Ig and EGF homology domains 1) and TIE-2/Tek comprise a receptor tyrosine kinase (RTK) subfamily with unique structural characteristics: two immunoglobulin-like domains flanking three epidermal growth factor (EGF)-like domains and followed by three fibronectin type III-like repeats in the extracellular region and a split tyrosine kinase domain in the cytoplasmic region. These receptors are expressed primarily on endothelial and hematopoietic progenitor cells and play critical roles in angiogenesis, vasculogenesis and hematopoiesis. Human TIE-1 cDNA encodes a 1122 amino acid (aa) residue precursor protein with an 18 residue putative signal peptide, a 726 residue extracellular domain and a 353 residue cytoplasmic domain. Two ligands, angiopoietin-1 (Ang1) and angiopoietin-2 (Ang2), which bind TIE-2 with high-affinity have been identified. Ang2 has been reported to act as an antagonist for Ang1. Mice engineered to overexpress Ang2 or to lack Ang1 or Tie-1 display similar angiogenic defects.
Synonyms
Angiopoietin-1 receptor precursor, Tyrosine-protein kinase receptor TIE-2, hTIE2, Tyrosine-protein kinase receptor TEK, p140 TEK, Tunica interna endothelial cell kinase, CD202b, VMCM, VMCM1, TIE2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized sTIE-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TEK 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 TIE-2 Fc Chimera in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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-Colony Stimulating Factor Pegylated Human Recombinant

CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

Product # :

CYT-018

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Description

Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8kDa. The Pegylated G-CSF is produced by attaching a 20kDa methoxypolyethylene glycol propionaldehyde (mPEG-ALD) to the N-terminal amino acid of G-CSF giving a total molecular mass of 38.8kDa. G-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

G-CSF is supplied in solution (0.69mg/ml) containing 10mM Acetate Buffer (pH 4.0), and 0.004% Polysorbate 80.

Purity

Greater than 95.0% as determined by SEC-HPLC.

Biological Activity

The ED₅₀, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

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Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Physical Appearance
Colorless, clear and transparent solution.
Stability
G-CSF PEG should be stored refrigerated at 2° to 8°C. Vials should be kept in theirpackaging to protect from light until the time of use. Shaking and freezing should be avoided.
Background
What is the molecular weight/Mw of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein has a total Mw of 18.8kDa.

What is the source or expression system of G CSF HUMAN, PEG Protein?
Escherichia Coli.

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

What is the Biological Activity of G CSF HUMAN, PEG Protein?
The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

What is the amino acid sequence of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein is composed from 175 amino acids.

What applications can G CSF HUMAN, PEG Protein be used in?
G CSF HUMAN, PEG Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for G CSF HUMAN, PEG Protein?
The endotoxin level is minimal, G CSF HUMAN, PEG 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:

Adiponectin glycosylated Human Recombinant, HMW Rich

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-764

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

Adiponectin Human Recombinant HMW Rich produced in HEK cells is a single, glycosylated, polypeptide chain (19-244) containing a total of 226 amino acids, having a molecular mass of 24.6kDa (calculated). Human Acrp30 HMW Rich migrates on SDS-PAGE under non-reducing conditions at ~ 884 kDa.

Source

HEK293.

Formulation

Acrp30 was filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris, 50mM NaCl, pH 7.5 and 1mM CaCl2.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein 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.
Solubility
It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Acrp30 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHITVYM KDVKVSLFKK DKAMLFTYDQ YQENNVDQAS GSVLLHLEVG DQVWLQVYGE GERNGLYADN DNDSTFTGFL LYHDTN.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 24.6 kDa.

What is the source or expression system of ADIPONECTIN Protein?
HEK293.

What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.

What is the amino acid sequence of ADIPONECTIN Protein?
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHITVYM KDVKVSLFKK DKAMLFTYDQ YQENNVDQAS GSVLLHLEVG DQVWLQVYGE GERNGLYADN DNDSTFTGFL LYHDTN.

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

What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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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