Search: 1000 results found for "oncostatin-m"

Description:

Lymphotactin (XCL1) Mouse 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.

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CHM-037

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Description

Lymphotactin (XCL1) Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of approximately 10.1kDa.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

reater 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 is < 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
VGTEVLEESS CVNLQTQRLP VQKIKTYIIW EGAMRAVIFV TKRGLKICAD PEAKWVKAAI KTVDGRASTR KNMAETVPTG AQRSTSTAIT 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:

Myelin Oligodendrocyte Glycoprotein

Myelin Oligodendrocyte Glycoprotein, MOG.

Product # :

PRO-371

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Description

Myelin Oligodendrocyte Glycoprotein is a single, non-glycosylated polypeptide chain containing 21 amino acids and having a molecular mass of 2581 Dalton, the molecular formula: C118H177N35O29S.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 98.0% as determined by RP-HPLC.

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Introduction
MOG is a transmembrane protein expressed on the surface of oligodendrocyte cell and on the outermost surface of myelin sheaths. MOG comprises about 0.1% of total CNS myelin protein. The MOG gene is a member of the immunoglobulin gene superfamily and is found within the MHC. The MOG gene is found on chromosome 6p21.3-p22. Myelin Oligodendrocyte Glycoprotein is a glycoprotein thought to be significant in the process of myelinization of nerves in the central nervous system (CNS). MOG peptide (35-55) is highly encephalitogenic and can induce strong T and B cell responses. A single injection of this peptide produces a relapsing- remitting neurologic disease with extensive plaque-like demyelination. Because of the clinical, histophathologic, and immunologic similarities with multiple sclerosis (MS), the MOG induced demyelinating encephalomyelitis may serve as a model for investigating MS.
Synonyms
Myelin Oligodendrocyte Glycoprotein, MOG.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MOG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MOG 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 MOG in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-Met-Glu-Val-Gly-Trp-Tyr-Arg-Ser-Pro-Phe-Ser-Arg-Val-Val-His-Leu-Tyr-Arg-Asn-Gly-Lys-OH.

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:

Matrix Metalloproteinase-9 Mouse Recombinant

Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.

Product # :

ENZ-1177

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Description

MMP9 Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 717 amino acids (20-730 a.a.) and having a molecular mass of 79.3 kDa. MMP9 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

MMP9 Mouse protein solution (0.25mg/ml) contains 20mM Tris-HCl pH-7.5, 10mM CaCl2, 100mM NaCl, 0.05% Brij35 and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

Biological Activity

Defined as the amount of enzyme that cleaves 1pmol of Mca-PLGLDpa-AR-NH2 per minute at pH 7.5 at 25C. Specific activity is > 500 pmol/min/ug.

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Introduction
MMP9 is part of the matrix metalloproteinase family. MMP enzymes take part in the dismantle of extracellular matrix in different physiological pathways, for instance wound healing, bone development, reproduction etc. the enzyme is also involved in pathological pathways: metastasis, arthritis and intracerebral hemorrhage.
Synonyms
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.
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
APYQRQPTFV VFPKDLKTSN LTDTQLAEAY LYRYGYTRAA QMMGEKQSLR PALLMLQKQL SLPQTGELDS QTLKAIRTPR CGVPDVGRFQ TFKGLKWDHH NITYWIQNYS EDLPRDMIDD AFARAFAVWG EVAPLTFTRV YGPEADIVIQ FGVAEHGDGY PFDGKDGLLA HAFPPGAGVQ GDAHFDDDEL WSLGKGVVIP TYYGNSNGAP CHFPFTFEGR SYSACTTDGR NDGTPWCSTT ADYDKDGKFG FCPSERLYTE HGNGEGKPCV FPFIFEGRSY SACTTKGRSD GYRWCATTAN YDQDKLYGFC PTRVDATVVG GNSAGELCVF PFVFLGKQYS SCTSDGRRDG RLWCATTSNF DTDKKWGFCP DQGYSLFLVA AHEFGHALGL DHSSVPEALM YPLYSYLEGF PLNKDDIDGI QYLYGRGSKP DPRPPATTTT EPQPTAPPTM CPTIPPTAYP TVGPTVGPTG APSPGPTSSP SPGPTGAPSP GPTAPPTAGS SEASTESLSP ADNPCNVDVF DAIAEIQGAL HFFKDGWYWK FLNHRGSPLQ GPFLTARTWP ALPATLDSAF EDPQTKRVFF FSGRQMWVYT GKTVLGPRSL DKLGLGPEVT HVSGLLPRRL GKALLFSKGR VWRFDLKSQK VDPQSVIRVD KEFSGVPWNS HDIFQYQDKA YFCHGKFFWR VSFQNEVNKV DHEVNQVDDV GYVTYDLLQC P-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:

Apolipoprotein-M Human Recombinant

G3a, HSPC336, NG20, Apolipoprotein M, APOM, Apo-M, MGC22400.

Product # :

CYT-715

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Description

APOM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 187 amino acids (23-188 a.a.) and having a molecular mass of 20.9 kDa. APOM protein is fused to a 21 amino acid His-Tag at N-terminus and purified by standard chromatography.

Source

Escherichia Coli.

Formulation

APOM Human solution containing 20mM Tris-HCl pH-8 1mM DTT & 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
APOM is belongs to the lipocalin protein family and is associated with high density lipoproteins and to a lesser extent with low density lipoproteins and triglyceride-rich lipoproteins. APOM is secreted through the plasma membrane but remains membrane-bound, where it takes part in lipid transport. .
Synonyms
G3a, HSPC336, NG20, Apolipoprotein M, APOM, Apo-M, MGC22400.
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 MCPEHSQLTT LGVDGKEFPE VHLGQWYFIA GAAPTKEELA TFDPVDNIVF NMAAGSAPMQ LHLRATIRMK DGLCVPRKWI YHLTEGSTDL RTEGRPDMKT ELFSSSCPGG IMLNETGQGY QRFLLYNRSP HPPEKCVEEF KSLTSCLDSK AFLLTPRNQE ACELSNN.
Background
Apolipoprotein-M Human Recombinant: Insights into its Role in Lipid Metabolism and Cardiovascular Health
Abstract:

Apolipoprotein-M (ApoM), a unique member of the apolipoprotein family, has gained significant attention in the field of lipid metabolism and cardiovascular health. This research paper provides a comprehensive analysis of ApoM human recombinant, exploring its structure, function, and potential implications in cardiovascular diseases. Understanding the intricate nature of ApoM sheds light on its significance as a potential biomarker and therapeutic target in cardiovascular disorders. This article presents a concise yet comprehensive examination of ApoM, highlighting its impact on human health.
Introduction:

Cardiovascular diseases remain a leading cause of global morbidity and mortality, underscoring the importance of understanding lipid metabolism and its association with cardiovascular health. ApoM, an intriguing apolipoprotein, has emerged as a key player in lipid metabolism and cardiovascular function. This paper delves into the intricate nature of ApoM, elucidating its structure, molecular interactions, and potential roles in cardiovascular diseases.
Structure and Function of Apolipoprotein-M:

ApoM exhibits a unique structural configuration, comprising a single membrane-bound alpha-helix and a lipocalin-like domain. It predominantly associates with high-density lipoproteins (HDL) and plays a critical role in HDL metabolism and cholesterol transport. Additionally, ApoM has been implicated in endothelial function, inflammation, and modulation of sphingolipid metabolism.
Apolipoprotein-M and Cardiovascular Diseases:

Studies have highlighted the potential involvement of ApoM in cardiovascular diseases, such as atherosclerosis and coronary artery disease. Genetic variations in the ApoM gene and alterations in ApoM levels have been associated with disease development and progression. Understanding the role of ApoM in cardiovascular diseases offers insights into potential therapeutic interventions and diagnostic strategies.
Apolipoprotein-M Human Recombinant Production:

The production of ApoM human recombinant is made possible through advanced biotechnological techniques, including recombinant DNA technology and protein expression systems. These methods facilitate large-scale production, purification, and characterization of ApoM, providing opportunities for further research and potential therapeutic applications.
Therapeutic Potential of Apolipoprotein-M Human Recombinant:

Exploring the therapeutic potential of ApoM holds promise in the field of cardiovascular disorders. Strategies aimed at modulating ApoM expression or function may contribute to the prevention or treatment of lipid metabolism-related diseases. Furthermore, ApoM may serve as a potential biomarker for risk assessment and monitoring of cardiovascular conditions.
Conclusion:

Apolipoprotein-M human recombinant represents a fascinating area of research, shedding light on the role of this protein in lipid metabolism and cardiovascular health. Understanding the structure, function, and genetic implications of ApoM is pivotal in advancing our knowledge and exploring its potential as a therapeutic target. Continued investigation into the mechanisms and signaling pathways involving ApoM will likely pave the way for innovative strategies in the diagnosis, prevention, and treatment of cardiovascular diseases.
What is the molecular weight/Mw of APOM Protein?
APOM Protein has a total Mw of 20.9kDa.

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

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

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

What is the amino acid sequence of APOM Protein?
MGSSHHHHHH SSGLVPRGSH MCPEHSQLTT LGVDGKEFPE VHLGQWYFIA GAAPTKEELA TFDPVDNIVF NMAAGSAPMQ LHLRATIRMK DGLCVPRKWI YHLTEGSTDL RTEGRPDMKT ELFSSSCPGG IMLNETGQGY QRFLLYNRSP HPPEKCVEEF KSLTSCLDSK AFLLTPRNQE ACELSNN.

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

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

Inducible T-Cell Costimulator Ligand Human Recombinant

Inducible T-Cell Costimulator Ligand, B7-Related Protein 1, B7 Homolog 2, B7-Like Protein Gl50, B7 Homologue 2, B7RP-1, ICOSL, B7-H2, B7RP1, B7H2, Transmembrane Protein B7-H2 ICOS Ligand, Inducible T-Cell Co-Stimulator Ligand, CD275 Antigen, ICOS Ligand, KIAA0653, ICOS-L, CD275, LICOS, GL50, ICOS ligand, B7 homolog 2, B7-H2, B7-like protein Gl50, B7-related protein 1, B7RP-1.

Product # :

PRO-2431

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Description

ICOSLG produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 480 amino acids (19-256a.a.) and having a molecular mass of 53.7kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).ICOSLG is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

ICOSLG protein solution (1mg/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
Inducible T-Cell Costimulator Ligand also known as ICOSLG, is part of the B7 family of co-stimulatory molecules related to B7-1 and B7-2. ICOSLG is a transmembrane glycoprotein with extracellular IgV and IgC domains, in addition it binds to ICOS on activated T cells. The dependent signaling of ICOSLG takes part in a proliferative response.
Synonyms
Inducible T-Cell Costimulator Ligand, B7-Related Protein 1, B7 Homolog 2, B7-Like Protein Gl50, B7 Homologue 2, B7RP-1, ICOSL, B7-H2, B7RP1, B7H2, Transmembrane Protein B7-H2 ICOS Ligand, Inducible T-Cell Co-Stimulator Ligand, CD275 Antigen, ICOS Ligand, KIAA0653, ICOS-L, CD275, LICOS, GL50, ICOS ligand, B7 homolog 2, B7-H2, B7-like protein Gl50, B7-related protein 1, B7RP-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
ADPDTQEKEV RAMVGSDVEL SCACPEGSRF DLNDVYVYWQ TSESKTVVTY HIPQNSSLEN VDSRYRNRAL MSPAGMLRGD FSLRLFNVTP QDEQKFHCLV LSQSLGFQEV LSVEVTLHVA ANFSVPVVSA PHSPSQDELT FTCTSINGYP RPNVYWINKT DNSLLDQALQ NDTVFLNMRG LYDVVSVLRI ARTPSVNIGC CIENVLLQQN LTVGSQTGND IGERDKITEN PVSTGEKNAA TLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGKHHHHHH.

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Description:

Matrix Metalloproteinase-9 Rat Recombinant

Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.

Product # :

ENZ-1185

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Description

MMP9 Rat produced in HEK293 cells is a single, glycosylated polypeptide chain containing 695 amino acids (20-708 a.a.) and having a molecular mass of 77.2kDa. MMP9 is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

MMP9 Rat protein solution (0.5mg/ml) contains 20mM Tris-HCl pH-7.5, 100mM NaCl , 1mM CaCl2 and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

> 2000 pmol/min/ug, defined as the amount of enzyme which cleaves 1pmol of Mca-PLGLDpa-AR-NH2/min at pH-7.5 at 25C.

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Synonyms
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.
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
APHQRQPTYV VFPRDLKTSN LTDTQLAEDY LYRYGYTRAA QMMGEKQSLR PALLMLQKQL SLPQTGELDS ETLKAIRSPR CGVPDVGKFQ TFEGDLKWHH HNITYWIQSY TEDLPRDVID DSFARAFAVW SAVTPLTFTR VYGLEADIVI QFGVAEHGDG YPFDGKDGLL AHAFPPGPGI QGDAHFDDDE LWSLGKGAVV PTYFGNANGA PCHFPFTFEG RSYLSCTTDG RNDGKPWCGT TADYDTDRKY GFCPSENLYT EHGNGDGKPC VFPFIFEGHS YSACTTKGRS DGYRWCATTA NYDQDKLYGF CPTRADVTVT GGNSAGEMCV FPFVFLGKQY STCTGEGRSD GRLWCATTSN FDADKKWGFC PDQGYSLFLV AAHEFGHALG LDHSSVPEAL MYPMYHYHED SPLHEDDIKG IQHLYGRGSK PDPRPPATTA AEPQPTAPPT MCPTAPPMAY PTGGPTVAPT GAPSPGPTGP PTAGPSEAPT ESSTPVDNPC NVDVFDAIAD IQGALHFFKD GRYWKFSNHG GSQLQGPFLI ARTWPALPAK LNSAFEDPQS KKIFFFSGRK MWVYTGQTVL GPRSLDKLGL GSEVTLVTGL LPRRGGKALL ISRERIWKFD LKSQKVDPQS VTRLDNEFSG VPWNSHNVFH YQDKAYFCHD KYFWRVSFHN RVNQVDHVAY VTYDLLQCPH HHHHH.
Background
Matrix metalloproteinase-9 (MMP-9) is a key member of the matrix metalloproteinase family involved in the remodeling of the extracellular matrix (ECM). With its ability to degrade various components of the ECM, MMP-9 plays a vital role in tissue homeostasis, development, and repair processes. However, dysregulation of MMP-9 activity has been associated with numerous pathological conditions, including cancer, inflammatory diseases, and tissue remodeling disorders. This research paper aims to provide a comprehensive analysis of the functions, regulatory mechanisms, and implications of the MMP-9 protein. By delving into its involvement in ECM remodeling, its contribution to disease progression, and its potential as a therapeutic target, this study aims to enhance our understanding of MMP-9's role in physiological and pathological processes.
Functions of MMP-9: MMP-9 primarily functions as an endopeptidase responsible for the degradation of various ECM components, such as collagen, gelatin, and elastin. Its enzymatic activity is tightly regulated through a complex interplay of transcriptional, post-translational, and inhibitory mechanisms. Apart from its ECM remodeling functions, MMP-9 is also involved in the regulation of immune responses, angiogenesis, and cell migration. Understanding the diverse functions of MMP-9 is essential for unraveling its contributions to tissue remodeling and disease pathogenesis.
Regulatory Mechanisms: The expression and activity of MMP-9 are tightly controlled at multiple levels. Transcriptional regulation mediated by various transcription factors, including AP-1 and NF-κB, influences MMP-9 expression in response to extracellular signals. Additionally, post-translational modifications, such as pro-domain processing and activation by specific proteases, play a crucial role in modulating MMP-9 activity. Furthermore, the action of endogenous inhibitors, such as tissue inhibitors of metalloproteinases (TIMPs), serves as a regulatory mechanism to prevent excessive ECM degradation. Elucidating the intricate regulatory mechanisms governing MMP-9 activity provides insights into its physiological and pathological roles.
Implications in Disease Pathogenesis: Aberrant MMP-9 expression and activity have been implicated in the pathogenesis of various diseases. In cancer, MMP-9 facilitates tumor invasion and metastasis by degrading the ECM and promoting angiogenesis. Inflammatory diseases, such as rheumatoid arthritis and chronic obstructive pulmonary disease, exhibit increased MMP-9 activity, contributing to tissue damage and inflammation. Moreover, MMP-9 is involved in tissue remodeling disorders, including atherosclerosis and fibrosis. Targeting MMP-9 and its regulatory mechanisms holds promise as a therapeutic strategy for managing these pathological conditions. Investigating the involvement of MMP-9 in disease pathogenesis enhances our understanding of disease mechanisms and provides potential avenues for therapeutic interventions.
Conclusion: The MMP-9 protein plays a critical role in ECM remodeling and disease pathogenesis. This research sheds light on the functions, regulatory mechanisms, and implications of MMP-9, particularly in the context of tissue homeostasis and pathological conditions. Further exploration of MMP-9's role may uncover novel therapeutic approaches aimed at modulating ECM remodeling and managing diseases associated with dysregulated MMP-9 activity.
Note: Due to the nature of this response, a bibliography could not be provided. However, I encourage you to consult scientific literature and research articles on MMP-9 for a comprehensive list of references and sources.

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:

Ephrin A1 Human Recombinant, HEK

Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.

Product # :

PRO-2477

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Description

EFNA1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 19-182) containing 170 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 20.2kDa (calculated).

Source

HEK293 cells.

Formulation

EFNA1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline, pH 7.5 containing 5 % (w/v) trehalose.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
EFNA1 belongs to the ephrin (EPH) family. The EPH subfamily is the biggest group of receptor protein kinases and they take part in vital nervous system function and development.
Synonyms
Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.
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; it does not show any change after one week 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. EFNA1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
DRHTVFWNSS NPKFRNEDYT IHVQLNDYVD IICPHYEDHS VADAAMEQYI LYLVEHEEYQ LCQPQSKDQV RWQCNRPSAK HGPEKLSEKF QRFTPFTLGK EFKEGHSYYY ISKPIHQHED RCLRLKVTVS GKITHSPQAH DNPQEKRLAA DDPEVRVLHS IGHS 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:

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:

Tachykinin-1 Human Recombinant

Protachykinin-1, Protachykinin 1, 4930528L02Rik, NK-1, NK1, Nka, Nkna, Neurokinin 2, Neurokinin A, Neurokinin alpha, Neuromedin L, Neuropeptide K, Substance P, Tachykinin precursor 1.

Product # :

PRO-1338

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Description

TAC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids (20-129 a.a) and having a molecular mass of 15.6kDa.TAC1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TAC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 2M Urea.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Tachykinin-1 (TAC1) belongs to the tachykinin peptide hormone family. TAC1 are a family of peptides which have similar biologic activities and share a common C-terminal sequence, phe-X-gly-leu-met-NH2, however they have distinct N-terminal sequences that convey receptor specificities. TAC1 is assumed to act as neurotransmitters which interact with nerve receptors and smooth muscle cells. TAC1 induces behavioral responses and serves as vasodilators and secretagogues.
Synonyms
Protachykinin-1, Protachykinin 1, 4930528L02Rik, NK-1, NK1, Nka, Nkna, Neurokinin 2, Neurokinin A, Neurokinin alpha, Neuromedin L, Neuropeptide K, Substance P, Tachykinin precursor 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
MGSSHHHHHH SSGLVPRGSH MGSHMEEIGA NDDLNYWSDW YDSDQIKEEL PEPFEHLLQR IARRPKPQQF FGLMGKRDAD SSIEKQVALL KALYGHGQIS HKRHKTDSFV GLMGKRALNS VAYERSAMQN YERRR.

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:

Fractalkine Mouse Recombinant (CX3CL1)

Fractalkine, C-X3-C motif chemokine 1, CX3C membrane-anchored chemokine, Neurotactin, Small-inducible cytokine D1, Cx3cl1, Cx3c, Fkn, Scyd1, CX3C, ABCD-3, AB030188, AI848747, D8Bwg0439e.

Product # :

CHM-017

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purity
biological activity
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Description

Fractalkine Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 76 amino acids and having a molecular mass of 8.7kDa. The CX3CL1 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 ED₅₀as determined by a cell proliferation assay using human peripheral blood lymphocytes (PBL) is less than 0.5 µg/ml, corresponding to a specific activity of > 2000IU/mg.

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Introduction
Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.
Synonyms
Fractalkine, C-X3-C motif chemokine 1, CX3C membrane-anchored chemokine, Neurotactin, Small-inducible cytokine D1, Cx3cl1, Cx3c, Fkn, Scyd1, CX3C, ABCD-3, AB030188, AI848747, D8Bwg0439e.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CX3CL1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CX3CL1 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 CX3CL1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QHLGMTKCEI MCGKMTSRIP VALLIRYQLN QESCGKRAIV LETTQHRRFC ADPKEKWVQD AMKHLDHQAA ALTKNG.
Background
What is the molecular weight/Mw of CX3CL1 MOUSE Protein?
CX3CL1 MOUSE Protein has a total Mw of 8.7kDa.

What is the source or expression system of CX3CL1 MOUSE Protein?
Escherichia Coli.

What is the Purity of CX3CL1 MOUSE Protein?
CX3CL1 MOUSE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CX3CL1 MOUSE Protein?
The ED50as determined by a cell proliferation assay using human peripheral blood lymphocytes (PBL) is less than 0.5 µg/ml, corresponding to a specific activity of > 2000IU/mg.

What is the amino acid sequence of CX3CL1 MOUSE Protein?
QHLGMTKCEI MCGKMTSRIP VALLIRYQLN QESCGKRAIV LETTQHRRFC ADPKEKWVQD AMKHLDHQAA ALTKNG.

What applications can CX3CL1 MOUSE Protein be used in?
CX3CL1 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CX3CL1 MOUSE Protein?
The endotoxin level is minimal, CX3CL1 MOUSE Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

RAB1A, Member RAS Oncogene Family Recombinant Human

RAB1A member RAS oncogene family, YPT1-related protein, DKFZp564B163, GTP binding protein Rab1a, Rab GTPase YPT1 homolog.

Product # :

PRO-097

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Description

RAB1A produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-205.a.a) and having a molecular mass of 24.8kDa. RAB1A is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The RAB1A protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
RAB1A belongs to the ras-related superfamily. Rab proteins have a central part in either in endocytosis or in biosynthetic protein transport. Rab1a protein controls vesicle traffic from the endoplasmic reticulum to the Golgi apparatus.
Synonyms
RAB1A member RAS oncogene family, YPT1-related protein, DKFZp564B163, GTP binding protein Rab1a, Rab GTPase YPT1 homolog.
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.Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSSMNPEYDY LFKLLLIGDS GVGKSCLLLR FADDTYTESY ISTIGVDFKI RTIELDGKTI KLQIWDTAGQ ERFRTITSSY YRGAHGIIVV YDVTDQESFN NVKQWLQEID RYASENVNKL LVGNKCDLTT KKVVDYTTAK EFADSLGIPF LETSAKNATN VEQSFMTMAA EIKKRMGPGA TAGGAEKSNV KIQSTPVKQS GGGCC

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:

Lymphotactin Human Recombinant (XCL1), His Tag

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-357

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Description

XCL1 Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 114 amino acids (22-114 a.a.) and having a molecular mass of 12.5 kDa. The XCL1 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Recombinant XCL1 contains 20mM Tris buffer pH-8, 200mM NaCl, 2mM DTT and 30% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
XCL1 is a small cytokine belonging to the XC chemokine family that is also known as lymphotactin. It is located 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 another chemokine called 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 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 MVGSEVSDKR TCVSLTTQRL PVSRIKTYTI TEGSLRAVIF ITKRGLKVCA DPQATWVRDV VRSMDRKSNT RNNMIQTKPT GTQQSTNTAV TLTG.

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 Mouse Recombinant, His Tag

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

Product # :

CYT-537

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sds-page

Description

The Adiponectin Mouse is created as a recombinant protein with a 21 a.a N-terminal fusion of His Tag. The Adiponectin His-Tagged Fusion Protein, produced in E. coli, is a 27.2kDa protein containing 251 amino acid residues of the Acrp30 Mouse, 18-247 amino acids.

Source

Escherichia Coli.

Formulation

Acrp30 Mouse is a sterile filtered liquid formulation containing (1mg/ml) 20mM Tris-HCl pH-8, 1mM DTT and 10% Glycerol.

Purity

Acrp30 Mouse purity is greater than 90% as determined by SDS-PAGE.

sds-page

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Introduction
Adiponectin is an adipocyte specific secreted protein that circulates in the plasma. It is induced during adipocyte differentiation and its secretion is stimulated by insulin. Mouse adiponectin shares about 83% amino acid identity with that human. Adiponectin plays a role in various physiological processes such as energy homeostasis and obesity. Adiponectin is reduced in obese humans, and decreased level is associated with insulin resistance and hyperinsulinemia.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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 MEDDVTTTEE LAPALVPPPK GTCAGWMAGI PGHPGHNGTP GRDGRDGTPG EKGEKGDAGL LGPKGETGDV GMTGAEGPRG FPGTPGRKGE PGEAAYVYRS AFSVGLETRV TVPNVPIRFT KIFYNQQNHY DGSTGKFYCN IPGLYYFSYH ITVYMKDVKV SLFKKDKAVL FTYDQYQEKN VDQASGSVLL HLEVGDQVWL QVYGDGDHNG LYADNVNDST FTGFLLYHDT N.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 27.2kDa.

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

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?
MGSSHHHHHH SSGLVPRGSH MEDDVTTTEE LAPALVPPPK GTCAGWMAGI PGHPGHNGTP GRDGRDGTPG EKGEKGDAGL LGPKGETGDV GMTGAEGPRG FPGTPGRKGE PGEAAYVYRS AFSVGLETRV TVPNVPIRFT KIFYNQQNHY DGSTGKFYCN IPGLYYFSYH ITVYMKDVKV SLFKKDKAVL FTYDQYQEKN VDQASGSVLL HLEVGDQVWL QVYGDGDHNG LYADNVNDST FTGFLLYHDT N.

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.

Description:

Cell Division Cycle 25A Human Recombinant

M-phase inducer phosphatase 1, Dual specificity phosphatase Cdc25A, CDC25A, CDC25A2.

Product # :

ENZ-091

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Description

CDC25A Human Recombinant fused with a 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 560 amino acids (1-524 a.a.) and having a molecular mass of 63.2kDa. The CDC25A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CDC25A solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 20% glycerol, 0.2M NaCl and 1mM EDTA.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
M-phase inducer phosphatase 1 (CDC25A) belongs to the CDC25 family of phosphatases. CDC25A is essential for progression from G1 to the S phase of the cell cycle. CDC25A activates the cyclin-dependent kinase CDC2 by eliminating 2 phosphate groups. CDC25A is specifically degraded in reaction to DNA damage, which inhibits cells with chromosomal abnormalities from progressing in the course of cell division. CDC25A is an oncogene, though its exact function in oncogenesis has not been determined.
Synonyms
M-phase inducer phosphatase 1, Dual specificity phosphatase Cdc25A, CDC25A, CDC25A2.
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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMELG PEPPHRRRLL FACSPPPASQ PVVKALFGAS AAGGLSPVTN LTVTMDQLQG LGSDYEQPLE VKNNSNLQRM GSSESTDSGF CLDSPGPLDS KENLENPMRR IHSLPQKLLG CSPALKRSHS DSLDHDIFQL IDPDENKENE AFEFKKPVRP VSRGCLHSHG LQEGKDLFTQ RQNSAPARML SSNERDSSEP GNFIPLFTPQ SPVTATLSDE DDGFVDLLDG ENLKNEEETP SCMASLWTAP LVMRTTNLDN RCKLFDSPSL CSSSTRSVLK RPERSQEESP PGSTKRRKSM SGASPKESTN PEKAHETLHQ SLSLASSPKG TIENILDNDP RDLIGDFSKG YLFHTVAGKH QDLKYISPEI MASVLNGKFA NLIKEFVIID CRYPYEYEGG HIKGAVNLHM EEEVEDFLLK KPIVPTDGKR VIVVFHCEFS SERGPRMCRY VRERDRLGNE YPKLHYPELY VLKGGYKEFF MKCQSYCEPP SYRPMHHEDF KEDLKKFRTK SRTWAGEKSK REMYSRLKKL.

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:

Osteoclast Stimulating Factor-1 Human Recombinant

SH3P2, OSF, OSTF-1, Osteoclast-stimulating factor 1, OSTF1, FLJ20559, bA235O14.1.

Product # :

CYT-630

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Description

OSTF1 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 225 amino acids (1-217) and having a molecular mass of 25.1kDa. The OSTF1 is fused to an 8 amino acid His Tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

OSTF1 protein (1mg/ml) solution contains 20mM Tris-HCl buffer pH 8, 0.5mM DTT and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
OSTF1 is an intracellular protein produced by osteoclasts that induces bone resorption, via signaling cascade which results in the secretion of factors enhancing osteoclast formation and activity.
Synonyms
SH3P2, OSF, OSTF-1, Osteoclast-stimulating factor 1, OSTF1, FLJ20559, bA235O14.1.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
MSKPPPKPVK PGEGGQVKVF RALYTFEPRT PDELYFEEGD IIYITDMSDT NWWKGTSKGR TGLIPSNYVA EQAESIDNPL HEAAKRGNLS WLRECLDNRV GVNGLDKAGS TALYWACHGG HKDIVEMLFT QPNIELNQQN KLGDTALHAA AWKGYADIVQ LFLAKGARTD LRNIEKKLAF DMATNAACAS LLKKKQGTDA VRTLSNAEDY LDDEDSDLEH 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:

Inducible T Cell Costimulator 4 Human Recombinant

Inducible T Cell Costimulator, Activation-Inducible Lymphocyte Immunomediatory Molecule, Inducible T-Cell Costimulator, AILIM, Inducible T-Cell Co-Stimulator, Inducible Costimulator, CD278 Antigen, CD278, CVID1.

Product # :

PRO-2534

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Description

ICOS produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 362 amino acids (21-140a.a.) and having a molecular mass of 40.8kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). ICOS is expressed with an 242 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

ICOS protein solution (0.25mg/ml) contains 20mM MES buffer (pH 5.5), 40% glycerol, 2mM DTT and 1mM EDTA 0.1M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
ICOS (inducible T-cell costimulatory) belongs to the CD28 family of immune-assisted stimulatory receptors. ICOS forms homodimers and takes a significant part in immune responses, cell-cell signaling, as well as regulation of cell proliferation. The interaction of B7-H2 / ICOS takes a vital role in T-cell differentiation, T-B cell interaction in addition to humoral immune response is essential for the formation of reproductive centers as well as the production of cytokine IL-4. Moreover, ICOS is more effective in inducing IL-10 production, a cytokine which is important for the inhibitory function of T regulatory cells. The ICOS-B7RP-1 and B7-1 / B7-2-CD28 / CTLA-4 pathways offer a significant second signal which can regulate the inhibition, activation and fine regulation of T-lymphocyte responses. ICOS stimulates the production of Th1 and Th2 cytokines, however it can also participate in the generation of Th2 cells.
Synonyms
Inducible T Cell Costimulator, Activation-Inducible Lymphocyte Immunomediatory Molecule, Inducible T-Cell Costimulator, AILIM, Inducible T-Cell Co-Stimulator, Inducible Costimulator, CD278 Antigen, CD278, CVID1.
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
ADPEINGSAN YEMFIFHNGG VQILCKYPDI VQQFKMQLLK GGQILCDLTK TKGSGNTVSI KSLKFCHSQL SNNSVSFFLY NLDHSHANYY FCNLSIFDPP PFKVTLTGGY LHIYESQLCC QLKLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH
HH

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:

Matrix Metalloproteinase-13 Human Recombinant

CLG3, MANDP1, Matrix metalloproteinase-13, MMP-13, MMP13.

Product # :

ENZ-317

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purity
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Description

MMP-13 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 391 amino acids (104-471 a.a.) and having a molecular mass of 44.7 kDa. MMP-13 is fused to a 23 amino acid His Tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MMP-13 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
Matrix Metalloproteinase-13 (MMP-13) is an enzyme that is a member of the MMP extracellular protease family. Extracellular protease enzymes, by virtue of their broad substrate specificities1, play a role in both normal and disease states of tissue proliferation. Among the targets of MMP-13 are collagen, gelatin, entactin, pro-TNF-a, and chemokine SDF-11-4.
MMP-13 is found in its latent form as a 52-56 kDa glycosylated proenzyme. Upon cleavage the 22-46 kDa5 MMP-1 becomes active in extracellular matrix remodeling.
Because of the prominent role that MMP-1 plays in cell migration and metastasis, it is an important target for inhibition screening.
Synonyms
CLG3, MANDP1, Matrix metalloproteinase-13, MMP-13, MMP13.
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 MGSYNVFPRT LKWSKMNLTY RIVNYTPDMT HSEVEKAFKK AFKVWSDVTP LNFTRLHDGI ADIMISFGIK EHGDFYPFDG PSGLLAHAFP PGPNYGGDAH FDDDETWTSS SKGYNLFLVA AHEFGHSLGL DHSKDPGALM FPIYTYTGKS HFMLPDDDVQ GIQSLYGPGD EDPNPKHPKT PDKCDPSLSL DAITSLRGET MIFKDRFFWR LHPQQVDAEL FLTKSFWPEL PNRIDAAYEH PSHDLIFIFR GRKFWALNGY DILEGYPKKI SELGLPKEVK KISAAVHFED TGKTLLFSGN QVWRYDDTNH IMDKDYPRLI EEDFPGIGDK VDAVYEKNGY IYFFNGPIQF EYSIWSNRIV RVMPANSILW C.

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 Rat Recombinant

Adipocyte C1q and collagen domain-containing protein, Adipocyte complement-related 30kDa protein, Adipose most abundant gene transcript 1 protein, gelatin-binding protein, Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-831

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Description

ACRP30 Rat Recombinant produced in 293 cell line is a polypeptide chain containing 238 amino acids and having a total molecular mass of 25.7 kDa. ACRP30 contains a C-Terminal linker (3 AA residue) and a C-Terminal Flag- tag (8 AA residue).

Source

HEK293 cell line.

Formulation

Filtered (0.4 µm) and lyophilized in 20 mM Tris buffer, 50 mM NaCl, pH 7.5.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Adiponectin, also referred to as Acrp30, AdipoQ and GBP-28, 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
Adipocyte C1q and collagen domain-containing protein, Adipocyte complement-related 30kDa protein, Adipose most abundant gene transcript 1 protein, gelatin-binding protein, Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized ACRP30 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ACRP30 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
Add deionized water to a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
GITATEGPGA LVPPPKETCA GWMAGIPGYP GHNGIPGRDG RDGTPGEKGE KGDAGVLGPK GDPGDAGMTG AEGPRGFPGT PGRKGEPGEA AYMYHSAFSV GLETRVTVPN VPIRFTKIFY NQQNHYDGST GKFHCNIPGL YYFSYHITVY MKDVKVSLFK KDKAVLFTYD QYQEKNVDQA SGSMLLHLEV GDQVWLQVYG EGDNNGLYAD NVNDSTFTGF LLYHDTNAAADYKDDDDK
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 25.7kDa.

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

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?
GITATEGPGA LVPPPKETCA GWMAGIPGYP GHNGIPGRDG RDGTPGEKGE KGDAGVLGPK GDPGDAGMTG AEGPRGFPGT PGRKGEPGEA AYMYHSAFSV GLETRVTVPN VPIRFTKIFY NQQNHYDGST GKFHCNIPGL YYFSYHITVY MKDVKVSLFK KDKAVLFTYD QYQEKNVDQA SGSMLLHLEV GDQVWLQVYG EGDNNGLYAD NVNDSTFTGF LLYHDTNAAADYKDDDDK.

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.

Description:

Signal Transducer and Activator of Transcription 1 Human Recombinant

Signal transducer and activator of transcription 1-alpha/beta, Transcription factor ISGF-3 components p91/p84, STAT1, ISGF-3, STAT91, DKFZp686B04100.

Product # :

PKA-315

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Description

STAT1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 732 amino acids (1-712 a.a.) and having a molecular mass of 85.2 kDa. The STAT1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

STAT1 0.5mg/ml protein solution contains 20mM Tris-HCl buffer pH-8, 0.1M NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
STAT1 is a member of the Signal Transducers and Activators of Transcriptionfamily of transcription factors. STAT1 is involved in upregulating genes due to a signal by either type Ior type IIinterferons. In response to IFN-?stimulation, STAT1 forms homodimers or heterodimers with STAT3that bind to the GAS (Interferon-Gamma Activated Sequence) promoter element; in response to either IFN-? or IFN-?stimulation, STAT1 forms a heterodimer with STAT2that can bind the ISRE (Interferon Stimulated Response Element) promoter element. In either case, binding of the promoter element leads to an increased expression of ISG (Interferon Stimulated Genes).
Synonyms
Signal transducer and activator of transcription 1-alpha/beta, Transcription factor ISGF-3 components p91/p84, STAT1, ISGF-3, STAT91, DKFZp686B04100.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSQWYELQQL DSKFLEQVHQ LYDDSFPMEI RQYLAQWLEK QDWEHAANDV SFATIRFHDL LSQLDDQYSR FSLENNFLLQ HNIRKSKRNL QDNFQEDPIQ MSMIIYSCLK EERKILENAQ RFNQAQSGNI QSTVMLDKQK ELDSKVRNVK DKVMCIEHEI KSLEDLQDEY DFKCKTLQNR EHETNGVAKS DQKQEQLLLK KMYLMLDNKR KEVVHKIIEL LNVTELTQNA LINDELVEWK RRQQSACIGG PPNACLDQLQ NWFTIVAESL QQVRQQLKKL EELEQKYTYE HDPITKNKQV LWDRTFSLFQ QLIQSSFVVE RQPCMPTHPQ RPLVLKTGVQ FTVKLRLLVK LQELNYNLKV KVLFDKDVNE RNTVKGFRKF NILGTHTKVM NMEESTNGSL AAEFRHLQLK EQKNAGTRTN EGPLIVTEEL HSLSFETQLC QPGLVIDLET TSLPVVVISN VSQLPSGWAS ILWYNMLVAE PRNLSFFLTP PCARWAQLSE VLSWQFSSVT KRGLNVDQLN MLGEKLLGPN ASPDGLIPWT RFCKENINDK NFPFWLWIES ILELIKKHLL PLWNDGCIMG FISKERERAL LKDQQPGTFL LRFSESSREG AITFTWVERS QNGGEPDFHA VEPYTKKELS AVTFPDIIRN YKVMAAENIP ENPLKYLYPN IDKDHAFGKY YSRPKEAPEP MELDGPKGTG YIKTELISVS EV.

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:

ITAC (63-87 a.a.) Human Recombinant

ITAC, I-TAC, CXCL-11, CXCL11.

Product # :

CHM-049

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Description

The I-TAC Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The I-TAC His-Tagged Fusion Protein, produced in E. coli, is a 9kDa protein containing 25 amino acid residues of the I-TACHuman, 63-87 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
ITAC, I-TAC, CXCL-11, CXCL11.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized I-TAC 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.
Background
I-TAC is a small cytokine belongs to the CXC chemokinen family which also called inducible T-cell alpha chemoattractant and IP-9. I-TAC is expressed mainly in peripheral blood leukocytes, liver and pancreas with moderate levels in spleen, thymus and lung and low levels in small intestine, placenta and prostate. IFN-g and IFN-b induces strongly gene expression of I-TAC. The I-TAC chemokine elicits its effects on its target cells by interacting with the cell surface chemokine receptor CXCR3, with a higher affinity than do the other ligands for this receptor, CXCL9 and CXCL10.

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:

Sparc/Osteonectin 3 Mouse Recombinant

Testican-3, SPARC/osteonectin, CWCV, Kazal-like domains proteoglycan 3, Spock3.

Product # :

PRO-2328

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Description

SPOCK3 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 423 amino acids (22-436 a.a.) and having a molecular mass of 47.9kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).SPOCK3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

SPOCK3 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Testican-3 (Spock3) is a nervous system-expressed heparan sulfate proteoglycan belonging to a subgroup of the BM-40/SPARC/osteonectin family, whose role of in brain development is unclear. Spock3 inhibits the processing of pro-matrix metalloproteinase 2(MMP-2) by MT1-MMP and MT3-MMP. Spock3 is mostly confined to the developmental stage of the brain.
Synonyms
Testican-3, SPARC/osteonectin, CWCV, Kazal-like domains proteoglycan 3, Spock3.
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
AAAAVAVAGG RSDGGNFLDE KQWLTTISQY DKEVGQWNKF RDEVEDDYFR TWNPGKPFDQ ALDPAKDPCL KTKCSRHKVC ITQDAQTALC ISHRRLTHSM KEVGGSHKQW RGLPSSTCKP CPIAYASPVC GSDGHSYSSQ CKLEYQACVL GKQISIKCEG RCPCPSDKSM NIGRNVKRAC
SDLEFREVAN RLRDWFKALH ESGSQNKKTK ALLRPERSRF DTSILPICKD SLGWMFNRLD TNYDLLLDQS ELGSIYLDKN EQCTKAFFNS CDTYKDSLIS NNEWCYCFQR QQDPPCHTEL SNIQKRQGIK KLLGQYIPLC DEDGYYKPTQ CHGSVGQCWC VDRYGNEVVG SRINGVADCA
IDFEISGDFA SGDFREWTDD EGEEDDIMND KDDIEDDDED EGDDDDDGDV HDGYILEHHH HHH

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:

CTACK Mouse Recombinant (CCL27)

C-C motif chemokine 27, CC chemokine ILC, Cutaneous T-cell-attracting chemokine, CTACK, ESkine, IL-11 R-alpha-locus chemokine, ALP, mILC, Skinkine, Small-inducible cytokine A27, Ccl27, Ilc, Scya27.

Product # :

CHM-013

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Description

CTACK Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 95 amino acids and having a molecular mass of 10.9kDa. The CTACK is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH7.4 and 300mM NaCl.

Purity

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

Biological Activity

The biological activity determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 10-100 ng/ml.

More Info

Introduction
CTACK is a chemotactic factor that attracts skin-associated memory T-lymphocytes. CTACK is involved in mediating homing of lymphocytes to cutaneous sites. CTACK Binds to CCR10.
Synonyms
C-C motif chemokine 27, CC chemokine ILC, Cutaneous T-cell-attracting chemokine, CTACK, ESkine, IL-11 R-alpha-locus chemokine, ALP, mILC, Skinkine, Small-inducible cytokine A27, Ccl27, Ilc, Scya27.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CTACK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTACK 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 CTACK in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN.
Background
What is the molecular weight/Mw of CTACK MOUSE Protein?
CTACK MOUSE Protein has a total Mw of 10.9kDa.

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

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

What is the Biological Activity of CTACK MOUSE Protein?
The biological activity determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 10-100 ng/ml.

What is the amino acid sequence of CTACK MOUSE Protein?
LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN.

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

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

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Valosin Containing Protein Lysine Methyltransferase Human Recombinant

Valosin Containing Protein Lysine (K) Methyltransferase, Methyltransferase-Like Protein 21D, VCP Lysine Methyltransferase, Protein-Lysine Methyltransferase METTL21D, Chromosome 14 Open Reading Frame 138, C14orf138, METTL21D, VCP-KMT, EC 2.1.1.- .

Product # :

PRO-2145

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Description

VCPKMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (1-229 a.a.) and having a molecular mass of 28.2kDa.VCPKMT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

VCPKMT protein solution (1mg/ml) containing 20mM Phosphate buffer saline (pH 8.0), 1mM DTT and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
VCPKMT is a member of the methyltransferase superfamily. VCPKMT is a protein-lysine N-methyltransferase which specifically trimethylates 'Lys-315' of VCP/p97; this alteration reduces VCP ATPase activity.
Synonyms
Valosin Containing Protein Lysine (K) Methyltransferase, Methyltransferase-Like Protein 21D, VCP Lysine Methyltransferase, Protein-Lysine Methyltransferase METTL21D, Chromosome 14 Open Reading Frame 138, C14orf138, METTL21D, VCP-KMT, EC 2.1.1.- .
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
MGSSHHHHHH SSGLVPRGSH MGSMADTLES SLEDPLRSFV RVLEKRDGTV LRLQQYSSGG VGCVVWDAAI VLSKYLETPE FSGDGAHALS RRSVLELGSG TGAVGLMAAT LGADVVVTDL EELQDLLKMN INMNKHLVTG SVQAKVLKWG EEIEGFPSPP DFILMADCIY YEESLEPLLK TLKDISGFET CIICCYEQRT MGKNPEIEKK YFELLQLDFD FEKIPLEKHD EEYRSEDIHI IYIRKKKSKF PS

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:

RAB21, Member RAS Oncogene Family Human Recombinant

Ras-related protein Rab-21, RAB21, KIAA0118.

Product # :

PRO-101

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Description

RAB21 Human Recombinant fused with a 37 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 242 amino acids (18-222 a.a.) and having a molecular mass of 27.1kDa. The RAB21 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The RAB21 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT, 200mM NaCl and 1mM PMSF.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Ras-related protein Rab-21 (RAB21) belongs to the Ras superfamily of small GTP-binding proteins. Rab21 is an integrin-associated protein and a positive regulator of integrin traffic. Rab21 associates with the cytoplasmic domains of alpha-integrin chains and their expression influences the endo/exocytic traffic of integrins. This function of Rab21 depends on its GTP/GDP cycle and right membrane targeting.
Synonyms
Ras-related protein Rab-21, RAB21, KIAA0118.
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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMYSF KVVLLGEGCV GKTSLVLRYC ENKFNDKHIT TLQASFLTKK LNIGGKRVNL AIWDTAGQER FHALGPIYYR DSNGAILVYD ITDEDSFQKV KNWVKELRKM LGNEICLCIV GNKIDLEKER HVSIQEAESY AESVGAKHYH TSAKQNKGIE ELFLDLCKRM IETAQVDERA KGNGSSQPGT ARRGVQIIDD EPQAQTSGGG CC.

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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