Search: 348 results found for "TIGAR"

Description:

Synaptotagmin XI Human Recombinant

Synaptotagmin XI, SytXI, Synaptotagmin 12, KIAA0080, SYT12, Synaptotagmin-11.

Product # :

PRO-2301

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Description

SYT11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 418 amino acids (37-431 a.a) and having a molecular mass of 47kDa. SYT11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

SYT11 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 50% glycerol.

Purity

Greater than 80% as determined by SDS-PAGE.

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Introduction
Synaptotagmin-11 (SYT11) protein may be involved in Ca2+-dependent exocytosis of secretory vesicles through Ca2+ and phospholipid binding to the C2 domain or may function as Ca2+ sensors in the process of vesicular trafficking and exocytosis.
Synonyms
Synaptotagmin XI, SytXI, Synaptotagmin 12, KIAA0080, SYT12, Synaptotagmin-11.
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 MGSWSCCHQQ AEKKQKNPPY KFIHMLKGIS IYPETLSNKK KIIKVRRDKD GPGREGGRRN LLVDAAEAGL LSRDKDPRGP SSGSCIDQLP IKMDYGEELR SPITSLTPGE SKTTSPSSPE EDVMLGSLTF SVDYNFPKKA LVVTIQEAHG LPVMDDQTQG SDPYIKMTIL PDKRHRVKTR VLRKTLDPVF DETFTFYGIP YSQLQDLVLH FLVLSFDRFS RDDVIGEVMV PLAGVDPSTG KVQLTRDIIK RNIQKCISRG ELQVSLSYQP VAQRMTVVVL KARHLPKMDI TGLSGNPYVK VNVYYGRKRI AKKKTHVKKC TLNPIFNESF IYDIPTDLLP DISIEFLVID FDRTTKNEVV GRLILGAHSV TASGAEHWRE VCESPRKPVA KWHSLSEY.

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

Description:

Interleukin-31 Canine Recombinant, HEK

IL-31, Interleukin 31, IL31.

Product # :

CYT-1215

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Description

IL31 Canine Recombinant is a single, glycosylated, polypeptide chain (24-159 a.a) containing a total of 136 amino acids, having a molecular mass of 25.2 kDa. IL31 is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The IL31 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Synonyms
IL-31, Interleukin 31, IL31.
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
SHMAPTHQLP PSDVRKIILE LQPLSRGLLE DYQKKETGVP ESNRTLLLCL TSDSQPPRLN SSAILPYFRA IRPLSDKNII DKIIEQLDKL KFQHEPETEI SVPADTFECK SFILTILQQF SACLESVFKS LNSGPQ.
Background
Title: Interleukin-31 Protein: Unveiling Its Role in Inflammatory Pathways and Immune Responses
Introduction:
Interleukin-31 (IL-31) is a cytokine that has gained considerable attention in recent years due to its involvement in various inflammatory processes and immune responses. Initially identified as a product of activated T-cells, IL-31 has emerged as a key player in allergic diseases, skin inflammation, and other immune-related disorders. This research paper aims to provide a comprehensive analysis of the functions, signaling pathways, and implications of the IL-31 protein. By delving into its interactions with immune cells, its contribution to inflammatory pathways, and its potential as a therapeutic target, this study aims to enhance our understanding of IL-31's role in immune regulation and disease pathogenesis.
Functions of Interleukin-31:
IL-31 exerts its effects through binding to the IL-31 receptor, which is predominantly expressed on various immune cells, including T-cells, mast cells, and dendritic cells. Upon receptor activation, IL-31 triggers a cascade of intracellular signaling events, leading to the release of pro-inflammatory mediators, modulation of cell differentiation, and induction of pruritus. Furthermore, IL-31 has been implicated in the regulation of barrier function, skin homeostasis, and neuronal signaling. Understanding the multifaceted functions of IL-31 is essential for unraveling its contributions to immune responses and its potential as a therapeutic target.
Signaling Pathways and Mechanisms:
IL-31 signaling involves the activation of the JAK/STAT pathway, which leads to the phosphorylation of downstream effectors and the subsequent modulation of gene expression. Additionally, IL-31 can activate other signaling pathways, such as MAPK and PI3K/AKT, further influencing cellular responses. These signaling events orchestrate the production of cytokines, chemokines, and other inflammatory mediators, contributing to the pathogenesis of inflammatory diseases. Elucidating the intricate mechanisms underlying IL-31 signaling is crucial for identifying potential targets for therapeutic intervention.
Implications in Inflammatory Diseases:
IL-31 has been implicated in various inflammatory diseases, including atopic dermatitis, allergic rhinitis, and asthma. Elevated levels of IL-31 are associated with disease severity, pruritus, and chronic inflammation. Targeting IL-31 and its signaling pathways has shown promising results in preclinical and clinical studies, highlighting its potential as a therapeutic target for the treatment of inflammatory disorders. Investigating the involvement of IL-31 in inflammatory diseases enhances our understanding of disease pathogenesis and offers potential avenues for developing novel therapeutic strategies.
Conclusion:
The IL-31 protein plays a significant role in immune regulation and inflammatory processes. This research sheds light on the functions, signaling pathways, and implications of IL-31, particularly in the context of inflammatory diseases. Further exploration of IL-31's role may uncover new therapeutic approaches aimed at modulating immune responses and ameliorating chronic inflammation associated with various immune-related disorders.
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 IL-31 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:

Thymopentin

Product # :

HOR-241

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Description

Thymopentin has a molecular formula of C30H49N9O9, Arg-Lys-Asp-Val-Tyr-OH having an Mw of 679.8 Dalton.

Formulation

The protein (1mg/ml) was lyophilized with no additives.

Purity

Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

What is the molecular weight/Mw of THYMOPENTIN Protein? THYMOPENTIN Protein has a total Mw of 0.67kDa. What is the Purity of THYMOPENTIN Protein? THYMOPENTIN Protein is >99% pure as determined by SDS-PAGE. What is the Biological Activity of THYMOPENTIN Protein? The biological functionality of THYMOPENTIN Protein will be determined in the future. What applications can THYMOPENTIN Protein be used in? THYMOPENTIN Protein can probably be used in western blot, ELISA and Lateral Flow. What is the endotoxin level for THYMOPENTIN Protein? The endotoxin level is minimal, THYMOPENTIN Protein was purified using conventional chromatography techniques.

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Introduction
Thymopentin, also known as TP-5, is a synthetic pentapeptide which is the active site of the naturally occurring hormone thymopoietin with immunomodulating properties (corresponding to the amino acids 32-36 of thymopoietin). Thymopentin enhances the production of thymic T cells and may help restore immunocompetence in immunosuppressed subjects. This agent also augments the effects of ionizing radiation by arresting cancer cells in the G2/M phase of the cell cycle.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Thymopentin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TP-5 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 Thymopentin in sterile 18MΩ-cm H2O not less than 100 µg/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:

Transforming Growth Factor-Beta 2 Mouse Recombinant

Transforming growth factor beta-2, TGF-beta-2, G-TSF, Tgfb-2, TGFbeta2.

Product # :

CYT-1266

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Description

Transforming Growth Factor-Beta 2 Mouse Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.4kDa.
TGFB2 Mouse Recombinant is purified by proprietary chromatographic techniques.

Source

CHO Cells.

Formulation

The protein was lyophilized with 0.1% (v/v) TFA and 35% (v/v) Acetonitrile.

Purity

Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.

Biological Activity

The biological activity was determined by TGFB2 ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells. The expected ED50 for this effect is <0.05ng/ml, corresponding to a specific activity of ≥ 2.0 × 107 units/mg.

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Synonyms
Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Transforming Growth Factor-Beta 2 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 Transforming Growth Factor-Beta 2 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHTK VLSLYNTINP EASASPCCVS QDLEPLTILY YIGNTPKIEQ LSNMIVKSCK CS.
Background
TGFB2 differ from TGFB1 in the tissue distribution, receptor interactions, and several biological roles.
TGFB2 requires TGFBR3 for its binding to TGFBR2 while TGFB1 binds directly to the receptor TGFBR2.
TGFB2 is crucial for embryonic development ocular biology, neural development, and tissue morphogenesis while TGFB1 is crucial for immune regulation and fibrosis.
TGFB2 exhibits more tissue-specific developmental expression Vs TGFB1.

What is the source or expression system of Mouse TGFB2 Protein?
CHO Cells

What is the Purity of Mouse TGFB2 Protein?
Mouse TGFB2 Protein is >97% pure as determined by SDS-PAGE.

What is the molecular weight / Mw of Mouse TGFB2 Protein?
Mouse TGFB2 Protein having a total Mw of 25.6kDa.

What is the Biological Activity of Mouse TGFB2 Protein?
The biological functionality of Mouse TGFB2 Protein is determined by mouse HT-2 cells.

What is the endotoxin level for Mouse TGFB2 Protein?
The endotoxin level is minimal, Mouse TGFB2 Protein was purified using conventional chromatography techniques.

What is the amino acid sequence of Mouse TGFB2 Protein?
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHTK VLSLYNTINP EASASPCCVS QDLEPLTILY YIGNTPKIEQ LSNMIVKSCK CS.

Is TGFB2 a homodimer / homodimeric protein?
Yes, TGFB2 is homo dimer consisting of 2 identical chains.

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:

SARS Associated Coronavirus Spike (14-1195 a.a.) Recombinant

Spike glycoprotein, S glycoprotein, Peplomer protein, E2 glycoprotein precursor, Severe acute repiratory Syndrome-related Coronavirus, SARS, SRAS-CoV, SARS-CoV1, E2.

Product # :

SARS-048

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Description

SARS Spike produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 1188 amino acids (14-1195 aa) and having a molecular mass of 131.9kDa.SARS Spike is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The SARS Spike (14-1195) solution (0.25mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% Glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

Biological Activity

Measured by its binding ability in a functional ELISA with Human ACE-2 (CAT# enz-1159).

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Introduction
SARS Coronavirus is an enveloped virus containing 3 outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. Accordingly, S-protein takes part in virus infection cycle and is the primary target of neutralizing antibodies.
Synonyms
Spike glycoprotein, S glycoprotein, Peplomer protein, E2 glycoprotein precursor, Severe acute repiratory Syndrome-related Coronavirus, SARS, SRAS-CoV, SARS-CoV1, E2.
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
SDLDRCTTFD DVQAPNYTQH TSSMRGVYYP DEIFRSDTLY LTQDLFLPFY SNVTGFHTIN HTFGNPVIPF KDGIYFAATE KSNVVRGWVF GSTMNNKSQS VIIINNSTNV VIRACNFELC DNPFFAVSKP MGTQTHTMIF DNAFNCTFEY ISDAFSLDVS EKSGNFKHLR EFVFKNKDGF LYVYKGYQPI DVVRDLPSGF NTLKPIFKLP LGINITNFRA ILTAFSPAQD IWGTSAAAYF VGYLKPTTFM LKYDENGTIT DAVDCSQNPL AELKCSVKSF EIDKGIYQTS NFRVVPSGDV VRFPNITNLC PFGEVFNATK FPSVYAWERK KISNCVADYS VLYNSTFFST FKCYGVSATK LNDLCFSNVY ADSFVVKGDD VRQIAPGQTG VIADYNYKLP DDFMGCVLAW NTRNIDATST GNYNYKYRYL RHGKLRPFER DISNVPFSPD GKPCTPPALN CYWPLNDYGF YTTTGIGYQP YRVVVLSFEL LNAPATVCGP KLSTDLIKNQ CVNFNFNGLT GTGVLTPSSK RFQPFQQFGR DVSDFTDSVR DPKTSEILDI SPCAFGGVSV ITPGTNASSE VAVLYQDVNC TDVSTAIHAD QLTPAWRIYS TGNNVFQTQA GCLIGAEHVD TSYECDIPIG AGICASYHTV SLLRSTSQKS IVAYTMSLGA DSSIAYSNNT IAIPTNFSIS ITTEVMPVSM AKTSVDCNMY ICGDSTECAN LLLQYGSFCT QLNRALSGIA AEQDRNTREV FAQVKQMYKT PTLKYFGGFN FSQILPDPLK PTKRSFIEDL LFNKVTLADA GFMKQYGECL GDINARDLIC AQKFNGLTVL PPLLTDDMIA AYTAALVSGT ATAGWTFGAG AALQIPFAMQ MAYRFNGIGV TQNVLYENQK QIANQFNKAI SQIQESLTTT STALGKLQDV VNQNAQALNT LVKQLSSNFG AISSVLNDIL SRLDKVEAEV QIDRLITGRL QSLQTYVTQQ LIRAAEIRAS ANLAATKMSE CVLGQSKRVD FCGKGYHLMS FPQAAPHGVV FLHVTYVPSQ ERNFTTAPAI CHEGKAYFPR EGVFVFNGTS WFITQRNFFS PQIITTDNTF VSGNCDVVIG IINNTVYDPL QPELDSFKEE LDKYFKNHTS PDVDLGDISG INASVVNIQK EIDRLNEVAK NLNESLIDLQ ELGKYEQYIK WPHHHHHH

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:

Regulator of G-Protein Signaling 16 Human Recombinant

A28-RGS14, A28-RGS14P, RGS-R, Regulator of G-protein signaling 16, RGS16, Retinally abundant regulator of G-protein signaling, Retinal-specific RGS, hRGS-r, RGSR.

Product # :

PRO-798

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Description

RGS16 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 222 amino acids (1-202 a.a.) and having a molecular mass of 24.9 kDa. The RGS16 is fused to a 20 amino acid His Tag at N-terminal and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The RGS16 solution (0.5mg/ml) contains Phosphate Buffered Saline (pH7.4), 0.1M NaCl and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
RGS16 is part of the ''regulator of G protein signaling'' family. RGS16 inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. RGS16 Binds to G(i)-alpha and G(o)-alpha, but not to G(s)-alpha. RGS16 regulates the kinetics of signaling in the phototransduction cascade.
Synonyms
A28-RGS14, A28-RGS14P, RGS-R, Regulator of G-protein signaling 16, RGS16, Retinally abundant regulator of G-protein signaling, Retinal-specific RGS, hRGS-r, RGSR.
Physical Appearance
Sterile Filtered clear colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MCRTLAAFPT TCLERAKEFK TRLGIFLHKS ELGCDTGSTG KFEWGSKHSK ENRNFSEDVL GWRESFDLLL SSKNGVAAFH AFLKTEFSEE NLEFWLACEE FKKIRSATKL ASRAHQIFEE FICSEAPKEV NIDHETRELT RMNLQTATAT CFDAAQGKTR TLMEKDSYPR FLKSPAYRDL AAQASAASAT LSSCSLDEPS HT.

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:

Flt3-Ligand Human Recombinant, HEK derived

Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.

Product # :

CYT-706

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Description

Flt3-Ligand Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 24-30kDa due to glycosylation. The Flt3-Ligand is purified by proprietary chromatographic techniques.

Source

HEK293 (Human Embryonic Kidney cell line).

Formulation

Flt3-Ligand was lyophilized from a 0.2µm filtered solution containing 1xPBS.

Purity

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

Biological Activity

The activity was determined by the dose- dependent stimulation of the proliferation of the human acute myeloid leukemia cell line OCI-AML5. The ED₅₀ is 0.56ng/ml.

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Introduction
FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.
Synonyms
Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3-Ligand 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 Flt3-Ligand in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTAPQP.
Background
What is the molecular weight/Mw of FLT3 LIGAND HUMAN, HEK Protein?
FLT3 LIGAND HUMAN, HEK Protein has a total Mw of 27kDa.

What is the source or expression system of FLT3 LIGAND HUMAN, HEK Protein?
HEK293 (Human Embryonic Kidney cell line).

What is the Purity of FLT3 LIGAND HUMAN, HEK Protein?
FLT3 LIGAND HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FLT3 LIGAND HUMAN, HEK Protein?
The activity was determined by the dose- dependent stimulation of the proliferation of the human acute myeloid leukemia cell line OCI-AML5. The ED50 is 0.56ng/ml.

What is the amino acid sequence of FLT3 LIGAND HUMAN, HEK Protein?
TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTAPQP.

What applications can FLT3 LIGAND HUMAN, HEK Protein be used in?
FLT3 LIGAND HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FLT3 LIGAND HUMAN, HEK Protein?
The endotoxin level is minimal, FLT3 LIGAND HUMAN, HEK 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:

Flt3 Ligand Mouse Recombinant, Sf9

Fms-related tyrosine kinase 3 ligand, Flt3 ligand, Flt3L, SL cytokine, lt3lgF, Flt3l.

Product # :

CYT-910

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Description

Flt3 Ligand produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (27-189 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 169 amino acids and having a molecular mass of 19.3kDa.Flt3 Ligand shows multiple bands between 18-28kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

Flt3 Ligand protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.
Synonyms
Fms-related tyrosine kinase 3 ligand, Flt3 ligand, Flt3L, SL cytokine, lt3lgF, Flt3l.
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
GTPDCYFSHS PISSNFKVKF RELTDHLLKD YPVTVAVNLQ DEKHCKALWS LFLAQRWIEQ LKTVAGSKMQ TLLEDVNTEI HFVTSCTFQP LPECLRFVQT NISHLLKDTC TQLLALKPCI GKACQNFSRC LEVQCQPDSS TLLPPRSPIA LEATELPEPR PRQHHHHHH
Background
What is the molecular weight/Mw of FLT3 LIGAND MOUSE, SF9 Protein?
FLT3 LIGAND MOUSE, SF9 Protein has a total Mw of 19.3kDa.

What is the source or expression system of FLT3 LIGAND MOUSE, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of FLT3 LIGAND MOUSE, SF9 Protein?
FLT3 LIGAND MOUSE, SF9 Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of FLT3 LIGAND MOUSE, SF9 Protein?
The biological functionality of FLT3 LIGAND MOUSE, SF9 Protein will be determined in the future.

What is the amino acid sequence of FLT3 LIGAND MOUSE, SF9 Protein?
GTPDCYFSHS PISSNFKVKF RELTDHLLKD YPVTVAVNLQ DEKHCKALWS LFLAQRWIEQ LKTVAGSKMQ TLLEDVNTEI HFVTSCTFQP LPECLRFVQT NISHLLKDTC TQLLALKPCI GKACQNFSRC LEVQCQPDSS TLLPPRSPIA LEATELPEPR PRQHHHHHH.

What applications can FLT3 LIGAND MOUSE, SF9 Protein be used in?
FLT3 LIGAND MOUSE, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FLT3 LIGAND MOUSE, SF9 Protein?
The endotoxin level is minimal, FLT3 LIGAND MOUSE, SF9 Protein was purified using conventional chromatography techniques.

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

Description:

HIV-1 TAT Clade-B Recombinant

Product # :

HIV-129

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Shipped at Room temp

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Description

HIV-1 TAT Recombinant- produced in E.coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids encoded by two exons and having a molecular mass of 14kDa.

Source

Escherichia Coli.

Formulation

Lyophilized with 0.1% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Human immunodeficiency virus type-1 (HIV-1) regulatory Tat protein plays an essential role in viral replication (Jones KA, 1994) and infectivity (Arya SK, 1985; Fisher AG, 1986). In addition, during acute infection, Tat is released extracellularly by infected cells (Chang HC, 1997; Ensoli B, 1990) and is taken up by neighboring cells where it transactivates viral replication (Ensoli B, 1993) and increases virus infectivity.
HIV-1 Tat activates transcription of HIV-1 viral genes by inducing phosphorylation of the C-terminal domain (CTD) of RNA polymerase II (RNAPII). Tat can also disturb cellular metabolism by inhibiting proliferation of antigen-specific T lymphocytes and by inducing cellular apoptosis. Tat-induced apoptosis of T-cells is attributed, in part, to the distortion of microtubules polymerization. LIS1 is a microtubule-associated protein that facilitates microtubule polymerization.
Physical Appearance
Sterile Filtered and lyophilized, though might appear as a solution as a result of the glycerol content.
Stability
Lyophilized HIV-1 TAT although stable at room temperature for 1 week, should be stored desiccated below -18°C. Upon reconstitution HIV-1 TAT 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 HIV-1 TAT in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MEPVDPRLEP WKHPGSQPKT ACTNCYCKKC CFHCQVCFIT KALGISYGRK KRRQRRRPPQ GSQTHQVSLS KQPTSQSRGD PTGPKE.
Specificity
Immunoreactive with all sera of HIV-1 infected individuals.

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:

Flt3 Ligand Human Recombinant

Fms-Related Tyrosine Kinase 3 Ligand, Flt3 Ligand, Flt-3 Ligand, SL Cytokine.

Product # :

CYT-331

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Description

Flt3-Ligand Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of approximately 17.6kDa. Flt3-Ligand is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized with no additives.

Purity

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

Biological Activity

The ED₅₀ as calculated by the dose-dependent stimulation of the proliferation of human AML5 cells is less than 1.0 ng/ml, corresponding to a Specific Activity of 1.0×10⁶ IU/mg.

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Introduction
FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.
Synonyms
Fms-Related Tyrosine Kinase 3 Ligand, Flt3 Ligand, Flt-3 Ligand, SL Cytokine.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3-Ligand 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 Flt3-L in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTA.
Background

What is the molecular weight/Mw of FLT3 LIGAND HUMAN Protein?
FLT3 LIGAND HUMAN Protein has a total Mw of 17.6kDa.

What is the source or expression system of FLT3 LIGAND HUMAN Protein?
Escherichia Coli.

What is the Purity of FLT3 LIGAND HUMAN Protein?
FLT3 LIGAND HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of FLT3 LIGAND HUMAN Protein?
The ED50 as calculated by the dose-dependent stimulation of the proliferation of human AML5 cells is less than 1.0 ng/ml, corresponding to a Specific Activity of 1.0×106 IU/mg.

What is the amino acid sequence of FLT3 LIGAND HUMAN Protein?
TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTA.

What applications can FLT3 LIGAND HUMAN Protein be used in?
FLT3 LIGAND HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FLT3 LIGAND HUMAN Protein?
The endotoxin level is minimal, FLT3 LIGAND HUMAN Protein was purified using conventional chromatography techniques.

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

Description:

Flt3 Ligand Human Recombinant, Sf9

Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.

Product # :

CYT-409

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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formulation
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biological activity
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Description

Flt3-Ligand Human Recombinant produced in Sf9 insect cells is a glycosylated, polypeptide chain containing 155 amino acids and having migrating on SDS-PAGE at 19kDa. Flt3-Ligand is purified by proprietary chromatographic techniques.

Source

Baculovirus Sf9 cells.

Formulation

The protein was lyophilized with no additives.

Purity

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

Biological Activity

The ED50, calculated by the dose-dependent stimulation of the proliferation of human MUTZ-2 cells is < 3.0 ng/ml.

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Introduction
FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.
Synonyms
Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3-L 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 Flt3-Ligand in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Thr-Gln-Asp-Cys-Ser.
Background
What is the molecular weight/Mw of FLT3 LIGAND HUMAN, SF9 Protein?
FLT3 LIGAND HUMAN, SF9 Protein has a total Mw of 19kDa.

What is the source or expression system of FLT3 LIGAND HUMAN, SF9 Protein?
Baculovirus Sf9 cells.

What is the Purity of FLT3 LIGAND HUMAN, SF9 Protein?
FLT3 LIGAND HUMAN, SF9 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FLT3 LIGAND HUMAN, SF9 Protein?
The ED50, calculated by the dose-dependent stimulation of the proliferation of human MUTZ-2 cells is < 3.0 ng/ml.

What is the amino acid sequence of FLT3 LIGAND HUMAN, SF9 Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Thr-Gln-Asp-Cys-Ser.

What applications can FLT3 LIGAND HUMAN, SF9 Protein be used in?
FLT3 LIGAND HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FLT3 LIGAND HUMAN, SF9 Protein?
The endotoxin level is minimal, FLT3 LIGAND HUMAN, SF9 Protein was purified using conventional chromatography techniques.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.42 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard of Flt3-Ligand as a Reference Standard.

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

Description:

Menopausal Gonadotropin Human

Product # :

HOR-251

Price :

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Description

Menopausal Gonadotropin Human is produced from a sterile preparation of placental glucoprotein urine of post-menopausal women.The MG is purified by proprietary chromatographic techniques.

Source

Urine of post-menopausal women.

Formulation

The Human MG was lyophilized from a concentrated (1mg/ml) solution with no additives.

Biological Activity

100 IU/mg of FSH and 100 IU/mg LH.

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Menopausal Gonadotropin Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MG 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 MG in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Contaminants
Free of: HbsAg, Hepatitis B surface antigen and antibodies to HIV, Hepatitis C and HIV.

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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