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Description:

Bone Morphogenetic protein-7 Human Recombinant, HEK

Osteogenic Protein 1, BMP-7.

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CYT-082

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Description

BMP-7 Human Recombinant produced in HEK cells is a glycosylated disulfide-linked homodimer, having a molecular weight range of 30-38kDa due to glycosylation.The BMP7 corresponds to amino acid residues 315 to 431 of the full-length BMP-7 precursor and is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

The BMP7 was lyophilized from 1mg/ml in 1xPBS.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

The specific activity was determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line (Mouse chondrogenic cell line) and is typically 50-250ng/ml.

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Introduction
The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.
Synonyms
Osteogenic Protein 1, BMP-7.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BMP7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-7 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 BMP-7 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DFSLDNEVHSSFIHRRLRSQERREMQREILSILGLPHRPRPHLQGKHNSAPMFMLDLYNAM AVEEGGGPGGQGFSYPYKAVFSTQGPPLASLQDSHFLTDADMVMSFVNLVEHDKEFFHPR YHHREFRFDLSKIPEGEAVTAAEFRIYKDYIRERFDNETFRISVYQVLQEHLGRESDLFLDSRTLWASE EGWLVFDITATSNHWVVNPRHNLGLQLSVETLDGQSINPKLAGLIGRHGPQNKQPFMVAFFKAT.
Background
BMP-7 Bone Morphogenetic Protein-7 Human Recombinant: A Key Regulator of Osteogenesis and Beyond
Abstract:
BMP-7 (Bone Morphogenetic Protein-7), also known as Osteogenic Protein 1 or BMP-7, is a potent growth factor that plays a crucial role in various biological processes, particularly in osteogenesis and tissue regeneration.
This research paper aims to comprehensively explore the molecular characteristics, signaling pathways, and diverse physiological functions of BMP-7.
Additionally, it investigates the therapeutic implications of BMP-7 in different disorders. Synonyms such as Osteogenic Protein 1 and BMP-7 associated with the protein are discussed throughout the paper to highlight their relevance in scientific literature.
Introduction:
BMP-7, also known as Osteogenic Protein 1 or BMP-7, is a growth factor with multifaceted roles in osteogenesis, tissue regeneration, and disease. This section introduces BMP-7 and its synonyms, highlighting their significance and relevance in scientific research.
Molecular Characteristics of BMP-7:
This section explores the molecular characteristics of BMP-7, including its primary amino acid sequence, protein structure, post-translational modifications, and binding partners. The importance of these factors in determining BMP-7's biological activity and receptor specificity is discussed.
Signaling Pathways Activated by BMP-7 :
BMP-7 activates specific signaling pathways upon binding to its receptors, leading to diverse cellular responses. This section focuses on the canonical BMP signaling pathway, highlighting the activation of Smad-dependent and Smad-independent pathways. The downstream effectors and transcriptional regulators involved in mediating BMP-7's cellular responses are also discussed.
Physiological Functions of BMP-7 :
BMP-7 plays critical roles in various physiological processes, particularly in osteogenesis and tissue regeneration. This section provides an in-depth analysis of BMP-7's contributions to these processes, emphasizing its role in promoting bone formation, cartilage development, renal function, and wound healing.
Therapeutic Implications of BMP-7 :
The unique properties of BMP-7 make it a promising therapeutic candidate for various disorders. This section discusses the potential applications of BMP-7 in bone regeneration, cartilage repair, kidney disease, and tissue engineering. The challenges and future directions in utilizing BMP-7 as a therapeutic agent are also explored.
BMP-7 in Disease Progression:
BMP-7 is implicated in the progression of certain diseases, including fibrosis, cancer, and cardiovascular disorders. This section examines the role of BMP-7 in tissue fibrosis, tumor progression, angiogenesis, and cardiac remodeling. The therapeutic implications and targeting of BMP-7 in disease management are also discussed.
Conclusion:
BMP-7, also known as Osteogenic Protein 1 or BMP-7, is a critical growth factor involved in osteogenesis, tissue regeneration, and disease progression. Understanding the molecular characteristics, signaling pathways, and physiological functions of BMP-7 contributes to the exploration of its therapeutic potential in various disorders.
What is the molecular weight/Mw of BMP7 Protein?
BMP7 Protein has a total Mw of 38kDa.

What is the source or expression system of BMP7 Protein?
HEK.

What is the Purity of BMP7 Protein?
BMP7 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BMP7 Protein?
The specific activity was determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line (Mouse chondrogenic cell line) and is typically 50-250ng/ml.

What is the amino acid sequence of BMP7 Protein?
DFSLDNEVHSSFIHRRLRSQERREMQREILSILGLPHRPRPHLQGKHNSAPMFMLDLYNAM AVEEGGGPGGQGFSYPYKAVFSTQGPPLASLQDSHFLTDADMVMSFVNLVEHDKEFFHPR YHHREFRFDLSKIPEGEAVTAAEFRIYKDYIRERFDNETFRISVYQVLQEHLGRESDLFLDSRTLWASE EGWLVFDITATSNHWVVNPRHNLGLQLSVETLDGQSINPKLAGLIGRHGPQNKQPFMVAFFKAT.

What applications can BMP7 Protein be used in?
BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMP7 Protein?
The endotoxin level is minimal, BMP7 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:

Beta-Secretase 2 Mouse Recombinant, HEK

BAE2, CDA13, CEAP1, DRAP, ARP1, ASP1, ASP21, 1110059C24Rik, AEPLC, AI850424, ALP56, beta-site APPcleaving enzyme 2, beta-secretase 2, Aspartyl protease 1, Asp 1, Beta-site amyloid precursor protein cleaving enzyme 2, Memapsin-1, Membrane-associated aspartic protease 1, Theta-secretase.

Product # :

ENZ-1188

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Description

BACE2 Mouse Recombinant produced in HEK293 Cells is a single, glycosylated, polypeptide chain (20-462 a.a) containing a total of 449 amino acids, having a molecular mass of 48.6 kDa. BACE2 Mouse is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

BACE2 (0.25mg/ml) is filtered in 10% (w/v) glycerol and Phosphate-Buffered Saline pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 20 pmol/min/ug in which one unit will convert 1.0pmole of Mca-SEVNLDAEFRK(Dnp)RR-NH2 to Mca- Pro-Leu-OH per minute at pH 3.5 at 25C.

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Synonyms
BAE2, CDA13, CEAP1, DRAP, ARP1, ASP1, ASP21, 1110059C24Rik, AEPLC, AI850424, ALP56, beta-site APPcleaving enzyme 2, beta-secretase 2, Aspartyl protease 1, Asp 1, Beta-site amyloid precursor protein cleaving enzyme 2, Memapsin-1, Membrane-associated aspartic protease 1, Theta-secretase.
Physical Appearance
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
AVPALAPAPF TLPLQVARAT NHRASAVPGL GTPELPRADG LALALEPVRA TANFLAMVDN LQGDSGRGYY LEMLIGTPPQ KVQILVDTGS SNFAVAGAPH SYIDTYFDSE SSSTYHSKGF DVTVKYTQGS WTGFVGEDLV TIPKGFNSSF LVNIATIFES ENFFLPGIKW NGILGLAYAA LAKPSSSLET FFDSLVAQAK IPDIFSMQMC GAGLPVAGSG TNGGSLVLGG IEPSLYKGDI
WYTPIKEEWY YQIEILKLEI GGQNLNLDCR EYNADKAIVD SGTTLLRLPQ KVFDAVVEAV ARTSLIPEFS DGFWTGAQLA CWTNSETPWA YFPKISIYLR DENASRSFRI TILPQLYIQP MMGAGFNYEC YRFGISSSTN ALVIGATVME GFYVVFDRAQ RRVGFAVSPC AEIEGTTVSE ISGPFSTEDI ASNCVPAQAL NEP HHHHHH.
Background
BACE2 protein, a member of the beta-secretase family, has gained attention as a key player in the pathogenesis of neurological disorders, particularly Alzheimer's disease. This research aims to explore the function and potential therapeutic implications of BACE2 protein in neurodegenerative conditions. Understanding the role of BACE2 protein can provide valuable insights into its significance as a therapeutic target for the development of novel treatment strategies.
Function of BACE2 Protein:
BACE2 is a transmembrane aspartic protease predominantly expressed in the central nervous system. It exhibits distinct cleavage activity on various protein substrates, including neuregulins, APP-like proteins, and TGF-β. Unlike its close homolog BACE1, BACE2 has been proposed to have non-amyloidogenic processing capabilities and has shown potential neuroprotective effects.
Implications of BACE2 Protein in Alzheimer's Disease:
Alzheimer's disease is characterized by the accumulation of amyloid-beta (Aβ) peptides in the brain, which are generated through the sequential cleavage of amyloid precursor protein (APP). BACE1 is primarily responsible for the cleavage of APP, leading to the production of toxic Aβ peptides. In contrast, BACE2 has been suggested to compete with BACE1, thereby reducing the levels of Aβ generation. This has led to speculation about the neuroprotective role of BACE2 and its potential as a therapeutic target for Alzheimer's disease.
BACE2 Protein and Neuronal Survival:
Emerging evidence suggests that BACE2 may play a role in promoting neuronal survival and function. Studies have shown that BACE2 deficiency leads to impaired synaptic plasticity, reduced dendritic branching, and altered neurotransmitter release. BACE2 has also been implicated in the regulation of axonal growth and guidance during development. These findings highlight the potential importance of BACE2 in maintaining neuronal integrity.
Association of BACE2 Protein with Other Neurological Disorders:
Apart from Alzheimer's disease, BACE2 has been implicated in other neurological conditions as well. Genetic studies have identified BACE2 gene variants associated with an increased risk of Parkinson's disease, suggesting its involvement in the pathogenesis of this disorder. Furthermore, BACE2 has been linked to the regulation of insulin signaling and glucose homeostasis, making it a potential target for diabetes-associated cognitive decline.
Therapeutic Implications of BACE2 Protein:
Given its potential neuroprotective effects and modulatory role in amyloid processing, BACE2 protein has emerged as a promising therapeutic target for neurodegenerative disorders. Strategies aimed at enhancing BACE2 activity or selectively activating BACE2-mediated non-amyloidogenic processing pathways hold promise for reducing amyloid pathology and preserving neuronal function. However, further research is needed to better understand the complex mechanisms underlying BACE2 function and to develop safe and effective therapeutic interventions.
Conclusion:
The investigation of BACE2 protein has provided valuable insights into its role in neurodegenerative diseases, particularly Alzheimer's disease. The potential neuroprotective effects and modulation of amyloid processing pathways by BACE2 make it an intriguing therapeutic target. Future studies should focus on unraveling the precise mechanisms by which BACE2 influences disease pathogenesis and developing strategies to harness its therapeutic potential. The exploration of BACE2 protein opens new avenues for the development of innovative treatment approaches for neurodegenerative disorders.

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:

Stem Cell Factor Rat Recombinant

Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250, Hematopoietic growth factor KL.

Product # :

CYT-323

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Description

Stem cell factor Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (26-189) and having a molecular mass of 18.4 kDa.The Rat SCF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 0.02% NaHCO3.

Purity

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

Biological Activity

The ED50 is determined by the dose-dependant stimulation of the proliferation of human TF-1 cells which is < 10 ng/ml, corresponding to a specific activity of 100,000units/mg.

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Introduction
Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117 (c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases.
SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid).
Synonyms
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250, Hematopoietic growth factor KL.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized rat SCF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCF 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 SCF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQEICRNPVT DNVKDITKLV ANLPNDYMIT LNYVAGMDVL PSHCWLRDMV THLSVSLTTL LDKFSNISEG LSNYSIIDKL GKIVDDLVAC MEENAPKNVK ESLKKPETRN FTPEEFFSIF NRSIDAFKDF MVASDTSDCV LSSTLGPEKD SRVSVTKPFM LPPVA.

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:

Leukemia Inhibitory Factor Mouse Recombinant

CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.

Product # :

CYT-645

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Description

Leukemia Inhibitory Factor (LIF) Murine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 181 amino acids and having a molecular mass of 20 kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Leukemia Inhibitory Factor (LIF) was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM Phosphate buffer pH-7.4 and 0.02% Tween-20.

Purity

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

Biological Activity

Activity of murine LIF was determined by the M1 cell differentiation assay which was found to be < 0.01 ng/ml, corresponding to a specific activity of 100,000,000 IU/mg.
A standard of 50 Units is defined as the concentration of mouse LIF in 1.0 mL of tissue culture medium that induces the differentiation of 50% of M1 colonies.

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Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
Synonyms
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leukemia Inhibitory Factor (LIF) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leukemia Inhibitory Factor (LIF) 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 Leukemia Inhibitory Factor (LIF) in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSPLPITPVNATCAIRHPCHGNLMNQIKNQLAQLNGSANALFISYYTAQGEPFP NNVEKLCAPNMTDFPSFHGNGTEKTKLVELYRMVAYLSASLTNITRDQKVLNP TAVSLQVKLNATIDVMRGLLSNVLCRLCNKYRVGHVDVPPVPDHSDKEAFQR KKLGCQLLGTYKQVISVVVQAF.

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:

RANK Human Recombinant

TNFRSF11A, ODFR, RANK, Tumor Necrosis Factor Receptor Superfamily, Member 11a, Activator Of NFKB, Receptor Activator Of Nuclear Factor-Kappa B, CD265 Antigen, LOH18CR1, TRANCER, CD265

Product # :

CYT-734

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Description

RANK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids and having a molecular mass of 19.1kDa. The RANK is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2 µm filtered concentrated solution in 20mM Tris-HCl, pH 8.0 and 150mM NaCl.

Purity

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

Biological Activity

The ED₅₀ as determined by its ability to inhibit sRANK Ligand induced nuclear factor kappa B (NFkappaB) in RAW 264.7 cells is less than 50 ng/ml, corresponding to a specific activity of
> 2.0 × 10⁴ IU/mg in the presence of 15 ng/ml of recombinant sRANK Ligand.

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Introduction
sRANK Receptor is a part of of the TNF superfamily of ligands and receptors which participates in the regulation of specific immunity and bone turnover. sRANK Receptor was originally acknowledged as a dendritic-cell-membrane protein, which by interacting with RANKL augments the capacity of dendritic cells to stimulate naive T cell proliferation and to endorse the survival of RANK and T cells. The full length human RANK cDNA encodes a type I transmembrane protein of 616 amino acids with a predicted 183 amino acid extracellular domain and a 383 amino acid cytoplasmic domain. sRANK Receptor is also expressed in a various tissues including skeletal muscle, thymus, liver, colon, small intestine and adrenal gland.
Synonyms
TNFRSF11A, ODFR, RANK, Tumor Necrosis Factor Receptor Superfamily, Member 11a, Activator Of NFKB, Receptor Activator Of Nuclear Factor-Kappa B, CD265 Antigen, LOH18CR1, TRANCER, CD265
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized RANK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution sRANK Receptor 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 RANK in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QIAPPCTSEK HYEHLGRCCN KCEPGKYMSS KCTTTSDSVC LPCGPDEYLD SWNEEDKCLL HKVCDTGKAL VAVVAGNSTT PRRCACTAGY HWSQDCECCR RNTECAPGLG AQHPLQLNKD TVCKPCLAGY FSDAFSSTDK CRPWTNCTFL GKRVEHHGTE KSDAVCSSSL PARK.

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:

Basigin Human Recombinant

Basigin isoform 2, 5F7, CD147, EMMPRIN, OK, TCSF, Leukocyte activation antigen M6, OK blood group antigen.

Product # :

PRO-2516

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Description

BSG produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 428 amino acids (22-207a.a.) and having a molecular mass of 47.5kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).BSG is expressed with a 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

BSG protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Basigin Isoform 2 or BSG is a part of the immunoglobulin superfamily, it is a type 1 transmembrane protein which has a variety of Nand O- glycosylation. BSG has several ligands, such as integrins, cyclophilin proteins Cyp-A & CyP-B. The protein has a crucial role in intercellular recognition, it takes part in many immunologic processes, differentiation and cell development. Also, it regulates numerus cell processes such as production and release of expression of the mono-carboxylate transporter, spermatogenesis, etc. Basigin Isoform 2 promotes invasion, metastasis, growth and survival of malignant cells by producing and releasing matrix metalloproteinases nearby mesenchymal cells and tumor cells.
Synonyms
Basigin isoform 2, 5F7, CD147, EMMPRIN, OK, TCSF, Leukocyte activation antigen M6, OK blood group antigen.
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
ADPAAGTVFT TVEDLGSKIL LTCSLNDSAT EVTGHRWLKG GVVLKEDALP GQKTEFKVDS DDQWGEYSCV FLPEPMGTAN IQLHGPPRVK AVKSSEHINE GETAMLVCKS ESVPPVTDWA WYKITDSEDK ALMNGSESRF FVSSSQGRSE LHIENLNMEA DPGQYRCNGT SSKGSDQAII
TLRVRSHLAL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG
QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH.

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:

IGF-Like Family Receptor 1 Human Recombinant

TMEM149, U2AF1L4, IGF-like family receptor 1, Transmembrane protein 149, U2 small nuclear RNA auxiliary factor 1-like 4, IGFLR1.

Product # :

PRO-1432

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Description

IGFLR1 Human Recombinant produced in E. coli is a single polypeptide chain containing 164 amino acids (23-163) and having a molecular mass of 17.5kDa. IGFLR1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The IGFLR1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.2M NaCl, 50% glycerol and 2mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
GF-like family receptor 1 (IGFLR1) is encoded by a gene mapping to human chromosome 19. IGFLR1 which is cell membrane receptor for the IGF-like family proteins binds IGFL1 and IGFL3 with a higher affinity and may as well bind IGFL2.
Synonyms
TMEM149, U2AF1L4, IGF-like family receptor 1, Transmembrane protein 149, U2 small nuclear RNA auxiliary factor 1-like 4, IGFLR1.
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 MGSSQYCGRL EYWNPDNKCC SSCLQRFGPP PCPDYEFREN CGLNDHGDFV TPPFRKCSSG QCNPDGAELC SPCGGGAVTP TPAAGGGRTP WRCRERPVPA KGHCPLTPGN PGAPSSQERS SPASSIAWRT PEPVPQQAWP NFLP.

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-3 Mouse Recombinant

MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

Product # :

CYT-371

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Description

Interleukin-3 mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids and having a molecular mass of 15100 Dalton. The IL-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

Purity

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

Biological Activity

The ED50 as determined by the dose-dependant stimulation of murine M-NFS-60 cells is < 0.05 ng/ml, corresponding to a Specific Activity of 20,000,000IU/mg.

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Introduction
Interleukin-3 is a pleiotropic cytokine produced primarily by activated T cells.
IL-3 is thought to function via specific cell surface receptors to stimulate the proliferation, differentiation and survival of haematopoietic cell lines. IL-3 has also been shown to affect the functional activity of a variety of other cell types including mast cells, eosinophils, megakaryocytes and basophils.
Synonyms
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-3 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 Interleukin-3 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 Met-Asp-Thr-His-Arg.
Background
What is the molecular weight/Mw of IL3 MOUSE Protein?
IL3 MOUSE Protein has a total Mw of 15.1kDa.

What is the source or expression system of IL3 MOUSE Protein?
Escherichia Coli.

What is the Purity of IL3 MOUSE Protein?
IL3 MOUSE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL3 MOUSE Protein?
The ED50 as determined by the dose-dependant stimulation of murine M-NFS-60 cells is < 0.05 ng/ml, corresponding to a Specific Activity of 20,000,000IU/mg.

What is the amino acid sequence of IL3 MOUSE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Asp-Thr-His-Arg.

What applications can IL3 MOUSE Protein be used in?
IL3 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL3 MOUSE Protein?
The endotoxin level is minimal, IL3 MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL3 MOUSE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL3 MOUSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.154 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL3 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:

Lymphocyte Antigen 86 Human Recombinant

Lymphocyte Antigen 86, MD-1 RP105-Associated, Protein MD-1, Ly-86, MMD-1, dJ80N2.1.

Product # :

PRO-1559

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Description

LY86 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (21-162) and having a molecular mass of 18.1kDa.LY86 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The LY86 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
LY86 is vital for effective CD180 cell surface expression and is vastly expressed in B-cells, tonsil and monocytes. LY86 collaborate with TLR4 and CD180 to facilitate the essential immune response to bacterial lipopolysaccharide (LPS) and cytokine production.
Synonyms
Lymphocyte Antigen 86, MD-1 RP105-Associated, Protein MD-1, Ly-86, MMD-1, dJ80N2.1.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. 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 MGSGGGGKAW PTHVVCSDSG LEVLYQSCDP LQDFGFSVEK CSKQLKSNIN IRFGIILRED IKELFLDLAL MSQGSSVLNF SYPICEAALP KFSFCGRRKG EQIYYAGPVN NPEFTIPQGE YQVLLELYTE KRSTVACANA TIMCS

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

Description:

Macrophage Inflammatory protein-3 (CCL19) Human Recombinant, T7 Tag

Small inducible cytokine A19, CCL19, Macrophage inflammatory protein 3 beta, MIP-3- beta, EBI1-ligand chemokine, ELC, Beta chemokine exodus-3, CK beta-11, chemokine (C-C motif) ligand 19, CKb11, MIP3B, MIP-3b, SCYA19, MGC34433, Epstein-Barr virus-induced molecule 1 ligand chemokine, EBI1-ligand chemokine.

Product # :

CHM-374

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SDS-PAGE
Citations

Description

MIP3b Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids (22-98 a.a.) and having a molecular mass of 10.4kDa.MIP3b is fused to a 16 amino acid T7-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MIP3b protein solution (0.5mg/ml) containing Phosphate Buffered Saline pH7.4 and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Chemokine (C-C motif) ligand 19 (CCL19) is a small cytokine belonging to the CC chemokine family that is also known as EBI1 ligand chemokine (ELC) and macrophage inflammatory protein-3-beta (MIP-3-beta). CCL19 is expressed abundantly in thymus and lymph nodes, with moderate levels in trachea and colon and low levels in stomach, small intestine, lung, kidney and spleen. The gene for CCL19 is located on human chromosome 9. This chemokine elicits its effects on its target cells by binding to the chemokine receptor chemokine receptor CCR7. It attracts certain cells of the immune system, including dendritic cells and antigen-engaged B cells.
Synonyms
Small inducible cytokine A19, CCL19, Macrophage inflammatory protein 3 beta, MIP-3- beta, EBI1-ligand chemokine, ELC, Beta chemokine exodus-3, CK beta-11, chemokine (C-C motif) ligand 19, CKb11, MIP3B, MIP-3b, SCYA19, MGC34433, Epstein-Barr virus-induced molecule 1 ligand chemokine, EBI1-ligand chemokine.
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
MASMTGGQQM GRGSHMGTND AEDCCLSVTQ KPIPGYIVRN FHYLLIKDGC RVPAVVFTTL RGRQLCAPPD QPWVERIIQR LQRTSAKMKR RSS.
Background
What is the molecular weight/Mw of CCL19 HUMAN, T7 Protein?
CCL19 HUMAN, T7 Protein has a total Mw of 10.4kDa.

What is the source or expression system of CCL19 HUMAN, T7 Protein?
Escherichia Coli.

What is the Purity of CCL19 HUMAN, T7 Protein?
CCL19 HUMAN, T7 Protein is > 95% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL19 HUMAN, T7 Protein?
The biological functionality of CCL19 HUMAN, T7 Protein will be determined in the future.

What is the amino acid sequence of CCL19 HUMAN, T7 Protein?
MASMTGGQQM GRGSHMGTND AEDCCLSVTQ KPIPGYIVRN FHYLLIKDGC RVPAVVFTTL RGRQLCAPPD QPWVERIIQR LQRTSAKMKR RSS.

What applications can CCL19 HUMAN, T7 Protein be used in?
CCL19 HUMAN, T7 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL19 HUMAN, T7 Protein?
The endotoxin level is minimal, CCL19 HUMAN, T7 Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL19 HUMAN, T7 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CCL19 HUMAN, T7?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Tetanus toxoid scFv Recombinant antibody

Product # :

ANT-195

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Quantity :

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Description

Tetanus toxin is the neurotoxin produced by the vegetative spore of Clostridium tetani in anaerobic conditions, causing tetanus.Recombinant Anti Tetanus produced in E.Coli is a non-glycosylated, polypeptide chain containing a hexahistidine tag and having a molecular weight of 37 kDa.Tetanus Antibody is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Tetanus is supplied in 1x PBS (pH 7.4) and 0.09% azide

Purity

Greater than 95.0% as determined byAnalysis by RP-HPLC.
Analysis by SDS-PAGE.

More Info

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.
Type
Antibody Recombinant.

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:

Toll Like Receptor 2 Human Recombinant

Toll Like Receptor 2, Toll/Interleukin-1 Receptor-Like Protein 4, Toll-Like Receptor 2, TIL4, CD282 Antigen, CD282, TLR2.

Product # :

PRO-2337

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Description

TLR2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 578 amino acids (21-588 aa) and having a molecular mass of 65.2kDa. TLR2 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TLR2 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
TLR2 belongs to the Toll-like receptor (TLR) family that plays a fundamental role in pathogen recognition and activation of innate immunity. TLRs are highly conserved from Drosophila to humans and share structural and functional similarities. They recognize pathogen-associated molecular patterns (PAMPs) which are expressed on infectious agents, and mediate the production of cytokines necessary for the development of effective immunity. The various TLRs exhibit different patterns of expression. TLR2 is expressed most abundantly in peripheral blood leukocytes, and mediates host response to Gram-positive bacteria and yeast via stimulation of NF-kappaB.
Synonyms
Toll Like Receptor 2, Toll/Interleukin-1 Receptor-Like Protein 4, Toll-Like Receptor 2, TIL4, CD282 Antigen, CD282, TLR2.
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
KEESSNQASL SCDRNGICKG SSGSLNSIPS GLTEAVKSLD LSNNRITYIS NSDLQRCVNL QALVLTSNGI NTIEEDSFSS LGSLEHLDLS YNYLSNLSSS WFKPLSSLTF LNLLGNPYKT LGETSLFSHL TKLQILRVGN MDTFTKIQRK DFAGLTFLEE LEIDASDLQS YEPKSLKSIQ NVSHLILHMK QHILLLEIFV DVTSSVECLE LRDTDLDTFH FSELSTGETN SLIKKFTFRN VKITDESLFQ VMKLLNQISG LLELEFDDCT LNGVGNFRAS DNDRVIDPGK VETLTIRRLH IPRFYLFYDL STLYSLTERV KRITVENSKV FLVPCLLSQH LKSLEYLDLS ENLMVEEYLK NSACEDAWPS LQTLILRQNH LASLEKTGET LLTLKNLTNI DISKNSFHSM PETCQWPEKM KYLNLSSTRI HSVTGCIPKT LEILDVSNNN LNLFSLNLPQ LKELYISRNK LMTLPDASLL PMLLVLKISR NAITTFSKEQ LDSFHTLKTL EAGGNNFICS CEFLSFTQEQ QALAKVLIDW PANYLCDSPS HVRGQQVQDV RLSVSECHRT LEHHHHHH

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:

Tyrosine Kinase ErbB-3 Human Recombinant, sf9

Tyrosine Kinase ErbB-3, sf9, ErbB3 sf9, Receptor tyrosine-protein kinase erbB-3, ERBB3, Proto-oncogene-like protein c-ErbB-3, Tyrosine kinase-type cell surface receptor HER3, HER3, Receptor tyrosine-protein kinase erbB-3 isoform, c-erbB-3, ErbB-3, erbB3-S, LCCS2, MDA-BF-1, p180-ErbB3, p45-sErbB3, p85-sErbB3.

Product # :

PKA-081

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Description

ErbB3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 863 amino acids (20-643 a.a.) and having a molecular mass of 95.6kDa (Migrates at 100-150kDa on SDS-PAGE under reducing conditions).ErbB3 is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

ErbB3 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
ErbB3, also called Her3 (human epidermal growth factor receptor 3), is a type I membrane glycoprotein that is a member of the ErbB family of tyrosine kinase receptors. ErbB family members serve as receptors for the epidermal growth factor (EGF) family of growth factors. Among ErbB family members, ErbB3 is unique in that it contains a defective kinase domain. ErbB3 is expressed in keratinocytes, melanocytes, skeletal muscle cells, embryonic myoblasts and Schwann cells. Monomeric ErbB3 serves as a low affinity receptor for the heregulins (HRG). ErbB3 can induce specific antibody production in vivo, hence to inhibit tumor cell growth. ErbB-3 can be used to treat early, medium and advanced or post-operative breast cancer with over-expression of ErbB2. According to its mechanism of action, ErbB3 is classified as a therapeutic for cancer.
Synonyms
Tyrosine Kinase ErbB-3, sf9, ErbB3 sf9, Receptor tyrosine-protein kinase erbB-3, ERBB3, Proto-oncogene-like protein c-ErbB-3, Tyrosine kinase-type cell surface receptor HER3, HER3, Receptor tyrosine-protein kinase erbB-3 isoform, c-erbB-3, ErbB-3, erbB3-S, LCCS2, MDA-BF-1, p180-ErbB3, p45-sErbB3, p85-sErbB3.
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
SEVGNSQAVC PGTLNGLSVT GDAENQYQTL YKLYERCEVV MGNLEIVLTG HNADLSFLQW IREVTGYVLV AMNEFSTLPL PNLRVVRGTQ VYDGKFAIFV MLNYNTNSSH ALRQLRLTQL TEILSGGVYI EKNDKLCHMD TIDWRDIVRD RDAEIVVKDN GRSCPPCHEV CKGRCWGPGS EDCQTLTKTI CAPQCNGHCF GPNPNQCCHD ECAGGCSGPQ DTDCFACRHF NDSGACVPRC PQPLVYNKLT FQLEPNPHTK YQYGGVCVAS CPHNFVVDQT SCVRACPPDK MEVDKNGLKM CEPCGGLCPK ACEGTGSGSR FQTVDSSNID GFVNCTKILG NLDFLITGLN GDPWHKIPAL DPEKLNVFRT VREITGYLNI QSWPPHMHNF SVFSNLTTIG GRSLYNRGFS LLIMKNLNVT SLGFRSLKEI SAGRIYISAN RQLCYHHSLN WTKVLRGPTE ERLDIKHNRP RRDCVAEGKV CDPLCSSGGC WGPGPGQCLS CRNYSRGGVC VTHCNFLNGE PREFAHEAEC FSCHPECQPM EGTATCNGSG SDTCAQCAHF RDGPHCVSSC PHGVLGAKGP IYKYPDVQNE CRPCHENCTQ GCKGPELQDC LGQTLVLIGK THLTRSPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH 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:

Osteocrin Human Recombinant, HEK

Osteocrin, Musclin, OSTN.

Product # :

PRO-2818

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Description

Osteocrin Human Recombinant is a single, glycosylated, polypeptide chain (28-133 a.a) containing a total of 112 amino acids and having a molecular mass of 12.5 kDa. Osteocrin is fused to a 6 a.a His-Tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 range ≤ 20 ng/ml measured by its binding ability in a functional ELISA with Human NPRC.

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Synonyms
Osteocrin, Musclin, OSTN.
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
VDVTTTEAFD SGVIDVQSTP TVREEKSATD LTAKLLLLDE LVSLENDVIE TKKKRSFSGF GSPLDRLSAG SVDHKGKQRK VVDHPKRRFG IPMDRIGRNR LSNSRGHHHH HH.
Background
Research has demonstrated that osteocrin influences bone formation by enhancing the anabolic effects of osteoblasts, the cells responsible for new bone formation. In addition to its skeletal roles, osteocrin has been shown to regulate cardiovascular functions by modulating blood pressure and cardiac hypertrophy. Furthermore, emerging evidence suggests that osteocrin may play a role in the central nervous system, impacting cognitive function and neuroprotection.

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:

Tyrosine Kinase ErbB-4 Human Recombinant

Receptor tyrosine-protein kinase erbB-4, Proto-oncogene-like protein c-ErbB-4, Tyrosine kinase-type cell surface receptor HER4, p180erbB4, 4ICD, E4ICD, s80HER4, ERBB4, HER4, receptor tyrosine-protein kinase erbB-4 isoform JM-a/CVT-1, receptor tyrosine-protein kinase erbB-4, tyrosine kinase-type cell surface receptor HER4, avian erythroblastic leukemia viral (v-erb-b2) oncogene homolog 4, proto-oncogene-like protein c-ErbB-4, ALS19, v-erb-a erythroblastic leukemia viral oncogene homolog 4, v-erb-b2 avian erythroblastic leukemia viral oncogene homolog 4, human epidermal growth factor receptor 4.

Product # :

PKA-128

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Description

ErbB4 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 863 amino acids (26-649 a.a) and having a molecular mass of 96.6 kDa.ErbB4 is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The ErbB4 solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured by its binding ability in a functional ELISA with Human NRG1(CAT# cyt-1186). The ED50 range ≤ 0.2 ug/ml.

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Introduction
Tyrosine Kinase ErbB-4 (ErbB4) is a receptor tyrosine kinase that is a member of the epidermal growth factor receptor family whose members play a role as receptors for the EGF family of growth factors. ErbB4is a single-pass type I transmembrane protein with multiple furin-like cysteine rich domains,PDZ domain binding motif, a tyrosine kinase domain and a phosphotidylinositol-3 kinase binding site. ErbB4binds its ligands with low affinity and is expressed in normal skeletal muscle, heart, pituitary, brain and some breast carcinomas. Monomeric ErbB4 takes part in neuronal development and development of the heart and cancer.
Synonyms
Receptor tyrosine-protein kinase erbB-4, Proto-oncogene-like protein c-ErbB-4, Tyrosine kinase-type cell surface receptor HER4, p180erbB4, 4ICD, E4ICD, s80HER4, ERBB4, HER4, receptor tyrosine-protein kinase erbB-4 isoform JM-a/CVT-1, receptor tyrosine-protein kinase erbB-4, tyrosine kinase-type cell surface receptor HER4, avian erythroblastic leukemia viral (v-erb-b2) oncogene homolog 4, proto-oncogene-like protein c-ErbB-4, ALS19, v-erb-a erythroblastic leukemia viral oncogene homolog 4, v-erb-b2 avian erythroblastic leukemia viral oncogene homolog 4, human epidermal growth factor receptor 4.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
QSVCAGTENK LSSLSDLEQQ YRALRKYYEN CEVVMGNLEI TSIEHNRDLS FLRSVREVTG YVLVALNQFR YLPLENLRII RGTKLYEDRY ALAIFLNYRK DGNFGLQELG LKNLTEILNG GVYVDQNKFL CYADTIHWQD IVRNPWPSNL TLVSTNGSSG CGRCHKSCTG RCWGPTENHC QTLTRTVCAE QCDGRCYGPY VSDCCHRECA GGCSGPKDTD CFACMNFNDS GACVTQCPQT FVYNPTTFQL EHNFNAKYTY GAFCVKKCPH NFVVDSSSCV RACPSSKMEV EENGIKMCKP CTDICPKACD GIGTGSLMSA QTVDSSNIDK FINCTKINGN LIFLVTGIHG DPYNAIEAID PEKLNVFRTV REITGFLNIQ SWPPNMTDFS VFSNLVTIGG RVLYSGLSLL ILKQQGITSL QFQSLKEISA GNIYITDNSN LCYYHTINWT TLFSTINQRI VIRDNRKAEN CTAEGMVCNH LCSSDGCWGP GPDQCLSCRR FSRGRICIES CNLYDGEFRE FENGSICVEC DPQCEKMEDG LLTCHGPGPD NCTKCSHFKD GPNCVEKCPD GLQGANSFIF KYADPDRECH PCHPNCTQGC NGPTSHDCIY YPWTGHSTLP QHARLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH 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:

Interleukin-3 Rat Recombinant

MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

Product # :

CYT-383

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interleukin-3 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 144 amino acids and having a molecular mass of 16.3kDa. The IL-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin-3 Rat was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

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

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of the proliferation of thymidine uptake by murine MC-9 cells is < 10 ng/ml, corresponding to a specific activity of >1.0 x 10⁵ units/mg.

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Introduction
Interleukin-3 is a pleiotropic cytokine produced primarily by activated T cells.
IL-3 is thought to function via specific cell surface receptors to stimulate the proliferation, differentiation and survival of haematopoietic cell lines. IL-3 has also been shown to affect the functional activity of a variety of other cell types including mast cells, eosinophils, megakaryocytes and basophils.
Synonyms
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL3 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 Interleukin 3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MISDRGSDAH HLLRTLDCRT IALEILVKLP YPQVSGLNNS DDKANLRNST LRRVNLDEFL KSQEEFDSQD TTDIKSKLQK LKCCIPAAAS DSVLPGVYNK DLDDFKKKLR FYVIHLKDLQ PVSVSRPPQP TSSSDNFRPM TVEC.
Background
What is the molecular weight/Mw of IL 3 RAT Protein?
IL 3 RAT Protein has a total Mw of 16.3kDa.

What is the source or expression system of IL 3 RAT Protein?
Escherichia Coli.

What is the Purity of IL 3 RAT Protein?
IL 3 RAT Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 3 RAT Protein?
The ED50 as determined by the dose-dependent stimulation of the proliferation of thymidine uptake by murine MC-9 cells is < 10 ng/ml, corresponding to a specific activity of >1.0 x 105 units/mg.

What is the amino acid sequence of IL 3 RAT Protein?
MISDRGSDAH HLLRTLDCRT IALEILVKLP YPQVSGLNNS DDKANLRNST LRRVNLDEFL KSQEEFDSQD TTDIKSKLQK LKCCIPAAAS DSVLPGVYNK DLDDFKKKLR FYVIHLKDLQ PVSVSRPPQP TSSSDNFRPM TVEC.

What applications can IL 3 RAT Protein be used in?
IL 3 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 3 RAT Protein?
The endotoxin level is minimal, IL 3 RAT Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 3 RAT that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL 3 RAT?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Peptidoglycan Recognition Protein 1 Human Recombinant, HEK

PGLYRP, PGRP, PGRP-S, PGRPS, TAG7, TNFSF3L, Peptidoglycan recognition protein 1, peptidoglycan recognition protein short.

Product # :

PRO-2726

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Description

PGLYRP1 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 184 amino acids (22-196 a.a) and having a molecular mass of 20.5 kDa.PGLYRP1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The PGLYRP1 solution (0.25mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured by its binding ability in a functional ELISA with Peptidoglycan. The ED50 range ≤ 30 ng/ml.

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Introduction
Peptidoglycan Recognition Protein 1 (PGLYRP1) is a member of the N-acetylmuramoyl-L-alanine amidase 2 family. PGLYRP1 binds to peptidoglycan of bacteria and affects the peptidoglycan biosynthesis. PGLYRP1 displays bactericidal activity towards Gram-positive bacteria and is bacteriostatic towards Gram-negative bacteria. PGLYRP1 has a role in innate immunity. PGLYRP1 is highly expressed in the bone marrow, and weakly expressed in the kidney, liver, small intestine, spleen, thymus, peripheral leukocyte, lung, fetal spleen and neutrophils.
Synonyms
PGLYRP, PGRP, PGRP-S, PGRPS, TAG7, TNFSF3L, Peptidoglycan recognition protein 1, peptidoglycan recognition protein short.
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
DGSQETEDPA CCSPIVPRNE WKALASECAQ HLSLPLRYVV VSHTAGSSCN TPASCQQQAR NVQHYHMKTL GWCDVGYNFL IGEDGLVYEG RGWNFTGAHS GHLWNPMSIG ISFMGNYMDR VPTPQAIRAA QGLLACGVAQ GALRSNYVLK GHRDVQRTLS PGNQLYHLIQ NWPHYRSPHH HHHH

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

Description:

Thymus Expressed Chemokine Human Recombinant (CCL25)

C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.

Product # :

CHM-364

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Shipped at Room temp

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Description

TECK Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 14.2kDa. The TECK is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 20mM PB, pH 7.4, 150mM NaCl.

Purity

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

Biological Activity

Determined by its ability to chemoattract human monocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

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Introduction
CCL25 (Teck) is a novel CC chemokine, which is distantly related (about 20% amino acid sequence identity) to other CC chemokines. The mouse CCL25 cDNA has also been cloned and shown to encode a 144 a.a. protein, which exhibits 49% a.a. sequence identity to the human CCL25. Human and mouse CCL25 expression was shown to be greatly restricted to the thymus and small intestine. While dendritic cells are identified as the source of CCL25 production in the thymus, dendritic cells derived from bone marrow do not express CCL25. CCL25 signals through the CCR9 receptor. Teck is possibly involved in T-cell development.
Recombinant human and mouse Teck were shown to be chemotactic for activated macrophages, dendritic cells and thymocytes. The recombinant protein demonstrates chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritic cells but is inactive on peripheral blood lymphocytes and neutrophils.
Synonyms
C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TECK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TECK 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 TECK in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QGVFEDCCLA YHYPIGWAVL RRAWTYRIQE VSGSCNLPAA IFYLPKRHRK VCGNPKSREV QRAMKLLDAR NKVFAKLHHN MQTFQAGPHA VKKLSSGNSK LSSSKFSNPI SSSRKNVSLL ISANSGL.
Background
What is the molecular weight/Mw of CCL25 HUMAN Protein?
CCL25 HUMAN Protein has a total Mw of 14.2kDa.

What is the source or expression system of CCL25 HUMAN Protein?
Escherichia Coli.

What is the Purity of CCL25 HUMAN Protein?
CCL25 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL25 HUMAN Protein?
Determined by its ability to chemoattract human monocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

What is the amino acid sequence of CCL25 HUMAN Protein?
QGVFEDCCLA YHYPIGWAVL RRAWTYRIQE VSGSCNLPAA IFYLPKRHRK VCGNPKSREV QRAMKLLDAR NKVFAKLHHN MQTFQAGPHA VKKLSSGNSK LSSSKFSNPI SSSRKNVSLL ISANSGL.

What applications can CCL25 HUMAN Protein be used in?
CCL25 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL25 HUMAN Protein?
The endotoxin level is minimal, CCL25 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL25 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CCL25 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

GABA(A) Receptor-Associated Protein Like 1 Human Recombinant

Gamma-aminobutyric acid receptor-associated protein-like 1, Early estrogen-regulated protein, GABA(A) receptor-associated protein-like 1, Glandular epithelial cell protein 1, GEC-1, GABARAPL1, GEC1, ATG8, APG8L, ATG8B, ATG8L, APG8-LIKE.

Product # :

PRO-048

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Description

GABARAPL1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 137 amino acids (1-117 a.a.) and having a molecular mass of 16.2kDa (Molecular size on SDS-PAGE will appear higher). The GABARAPL1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GABARAPL1 solution (1 mg/ml) contains 20mM Tris buffer (pH 8.0), 10% glycerol, 1mM DTT and 0.1M NaCl.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
GABARAPL1 [Gamma-aminobutyric acid (GABA) receptor-associated protein-like 1] is a member of the MAP1 LC3 family. GABARAPL1 increases cell surface expression of kappa type opioid receptor through facilitating anterograde intracellular trafficking of the receptor.
Synonyms
Gamma-aminobutyric acid receptor-associated protein-like 1, Early estrogen-regulated protein, GABA(A) receptor-associated protein-like 1, Glandular epithelial cell protein 1, GEC-1, GABARAPL1, GEC1, ATG8, APG8L, ATG8B, ATG8L, APG8-LIKE.
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 MKFQYKEDHP FEYRKKEGEK IRKKYPDRVP VIVEKAPKAR VPDLDKRKYL VPSDLTVGQF YFLIRKRIHL RPEDALFFFV NNTIPPTSAT MGQLYEDNHE EDYFLYVAYS DESVYGK.

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:

Myeloid Differentiation Primary Response 88, Mouse Anti Human

Myeloid differentiation primary response protein MyD88, MYD88, MYD88D.

Product # :

ANT-464

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Shipped with Ice Packs

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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.01% Sodium Azide.

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Introduction
Myeloid differentiation primary response gene 88 (MYD88) is a cytosolic adapter protein, which has a central role in the innate and adaptive immune response. MYD88 functions as a vital signal transducer in the interleukin-1 and Toll-like receptor signaling pathways. MYD88 acts via IRAK1, IRAK2, IRF7 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. The MYD88 protein increases IL-8 transcription. MYD88 is involved in IL-18-mediated signaling pathway. MYD88 activates IRF1, resulting in its rapid migration into the nucleus to mediate an efficient induction of IFN-beta, NOS2/INOS, and IL12A genes. MYD88 is comprised of an N-terminal death domain and a C-terminal Toll-interleukin1 receptor domain. Patients with defects in the MYD88 gene have an increased susceptibility to pyogenic bacterial infections.
Synonyms
Myeloid differentiation primary response protein MyD88, MYD88, MYD88D.
Physical Appearance
Sterile Filtered colorless solution.
Immunogen
Anti-human MYD88 mAb, clone PAT22F11A, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human MYD88 protein 1-309 amino acids purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and Kappa light chain.
Clone
PAT22F11A.
Applications
The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
MYD88 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

Description:

Cell Division Cycle 34 Human Recombinant, His Tag

UB2R1, CDC-34, Ubiquitin-conjugating enzyme E2 R1, Ubiquitin-protein ligase R1, Ubiquitin-conjugating enzyme E2-32 kDa complementing, E2-CDC34, CDC34, EC 6.3.2.19, UBC3, UBE2R1.

Product # :

ENZ-355

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Description

CDC34 Human Recombinant protein fused to a 20 amino acid N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 256 amino acids (1-236 a.a.) and having a molecular mass of 28.9 kDa. CDC34 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CDC34 (1mg/ml) protein solution contains 20mM Tris-Hcl pH-8, 10% glycerol, 50mM NaCl and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
CDC34 is important in the control of cell cycle and DNA replication. Cdc34 in association with different E3 complexes, including SCF, has been shown to target many different substrates for ubiquitination and degradation during cell division, signal transduction, and development. Cdc34 substrates that have been characterized include I?B, B-Myb, Wee1, MyoD, ICERII?, ATF5, p27Xic1, and p27Kip1. Additionally, substrates such as ?-catenin, p21Cip1, E2F, cyclin E, and cyclin D are putative substrates of Cdc34 by virtue of their SCF requirement for proteolysis. Cdc34 has been demonstrated to self-associate through a domain in the C-terminus, and is phosphorylated and ubiquitinylated in vivo. This protein is useful for in vitro ubiquitinylation reactions.
Synonyms
UB2R1, CDC-34, Ubiquitin-conjugating enzyme E2 R1, Ubiquitin-protein ligase R1, Ubiquitin-conjugating enzyme E2-32 kDa complementing, E2-CDC34, CDC34, EC 6.3.2.19, UBC3, UBE2R1.
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 MARPLVPSSQ KALLLELKGL QEEPVEGFRV TLVDEGDLYN WEVAIFGPPN TYYEGGYFKA RLKFPIDYPY
SPPAFRFLTK MWHPNIYETG DVCISILHPP VDDPQSGELP SERWNPTQNV RTILLSVISL LNEPNTFSPA NVDASVMYRK WKESKGKDRE
YTDIIRKQVL GTKVDAERDG VKVPTTLAEY CVKTKAPAPD EGSDLFYDDY YEDGEVEEEA DSCFGDDEDD SGTEES.

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 (CX3CL1) Human Recombinant, Sf9

Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

Product # :

CHM-042

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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SDS-PAGE
Citations

Description

Fractalkine Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 323 amino acids (25-339aa) and having a molecular mass of 34.3kDa.Fractalkine is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

SDS-PAGE

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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. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.
Synonyms
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
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
QHHGVTKCNI TCSKMTSKIP VALLIHYQQN QASCGKRAII LETRQHRLFC ADPKEQWVKD
AMQHLDRQAA ALTRNGGTFE KQIGEVKPRT TPAAGGMDES VVLEPEATGE SSSLEPTPSS
QEAQRALGTS PELPTGVTGS SGTRLPPTPK AQDGGPVGTE LFRVPPVSTA ATWQSSAPHQ
PGPSLWAEAK TSEAPSTQDP STQASTASSP APEENAPSEG QRVWGQGQSP RPENSLEREE
MGPVPAHTDA FQDWGPGSMA HVSVVPVSSE GTPSREPVAS GSWTPKAEEP IHATMDPQRL GVLITPVPDA QAATRLEHHH HHH
Background
What is the molecular weight/Mw of CX3CL1 HUMAN, SF9 Protein?
CX3CL1 HUMAN, SF9 Protein has a total Mw of 34.3kDa.

What is the source or expression system of CX3CL1 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of CX3CL1 HUMAN, SF9 Protein?
CX3CL1 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CX3CL1 HUMAN, SF9 Protein?
The biological functionality of CX3CL1 HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of CX3CL1 HUMAN, SF9 Protein?
QHHGVTKCNI TCSKMTSKIP VALLIHYQQN QASCGKRAII LETRQHRLFC ADPKEQWVKD
AMQHLDRQAA ALTRNGGTFE KQIGEVKPRT TPAAGGMDES VVLEPEATGE SSSLEPTPSS
QEAQRALGTS PELPTGVTGS SGTRLPPTPK AQDGGPVGTE LFRVPPVSTA ATWQSSAPHQ
PGPSLWAEAK TSEAPSTQDP STQASTASSP APEENAPSEG QRVWGQGQSP RPENSLEREE
MGPVPAHTDA FQDWGPGSMA HVSVVPVSSE GTPSREPVAS GSWTPKAEEP IHATMDPQRL GVLITPVPDA QAATRLEHHH HHH

What applications can CX3CL1 HUMAN, SF9 Protein be used in?
CX3CL1 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CX3CL1 HUMAN, SF9 Protein?
The endotoxin level is minimal, CX3CL1 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant CX3CL1 HUMAN, SF9 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CX3CL1 HUMAN, SF9?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

CD4 (26-396) Human Recombinant

CD4 Molecule, T-Cell Surface Glycoprotein CD4, T-Cell Surface Antigen T4/Leu-3, CD4 Antigen (P55), CD4 Receptor, CD4 Antigen, CD4mut, T-cell surface glycoprotein CD4.

Product # :

CYT-885

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Description

CD4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 396 amino acids (26-396 a.a) and having a molecular mass of 44kDa. CD4 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

CD4 protein solution (0.25mg/ml) containing 20mM Tris Hcl, PH8.0 and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
CD4 is a cell-surface glycoprotein found on the mature helper T cells and immature thymocytes, as well as on monocytes and macrophages. (Some cytotoxic T cells have CD4 protein as well.) Normally, about 65% of T cells in the blood are CD4+ (have CD4 protein protruding from their membrane). A mature T cell with either have CD4 or CD8, but not both. During one stage of development T cells develop CD4 and CD8 receptors, but they eventually are differentiated in the thymus and become more specialized.
Synonyms
CD4 Molecule, T-Cell Surface Glycoprotein CD4, T-Cell Surface Antigen T4/Leu-3, CD4 Antigen (P55), CD4 Receptor, CD4 Antigen, CD4mut, T-cell surface glycoprotein CD4.
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 MGSHMKKVVL GKKGDTVELT CTASQKKSIQ FHWKNSNQIK ILGNQGSFLT KGPSKLNDRA DSRRSLWDQG NFPLIIKNLK IEDSDTYICE VEDQKEEVQL LVFGLTANSD THLLQGQSLT LTLESPPGSS PSVQCRSPRG KNIQGGKTLS VSQLELQDSG TWTCTVLQNQ KKVEFKIDIV VLAFQKASSI VYKKEGEQVE FSFPLAFTVE KLTGSGELWW QAERASSSKS WITFDLKNKE VSVKRVTQDP KLQMGKKLPL HLTLPQALPQ YAGSGNLTLA LEAKTGKLHQ EVNLVVMRAT QLQKNLTCEV WGPTSPKLML SLKLENKEAK VSKREKAVWV LNPEAGMWQC LLSDSGQVLL ESNIKVLPTW STPVQP.

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

Description:

Macrophage Inflammatory Protein-3 alpha Mouse Recombinant (CCL20)

Small inducible cytokine A20 precursor, CCL20, Macrophage inflammatory protein 3 alpha, MIP-3-alpha, Liver and activation- regulated chemokine, CC chemokine LARC, Beta chemokine exodus-1, CKb4, LARC, ST38, MIP3A, MIP-3a, SCYA20, C-C motif chemokine 20, CC chemokine ST38, exodus-1.

Product # :

CHM-236

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

Macrophage Inflammatory Protein-3 alpha Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.9 kDa. The MIP-3a is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

Purity

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

Biological Activity

The Activity is calculated by its ability to chemoattract primary human T cells at 2-20ng/ml, corresponding to a specific activity of 50,000-500,000 units/mg.

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Introduction
CCL20 is a chemotactic factor that draws lymphocytes & neutrophils, rather than monocytes. MIP-3 alpha inhibits proliferation of myeloid progenitors in colony formation assays. MIP3A plays a role in the formation and function of the mucosal lymphoid tissues by attracting lymphocytes and dendritic cells towards epithelial cells. C-terminal processed forms have been shown to be equally chemotactically active for leukocytes. CCL20 holdes antibacterial activity e.coli atcc 25922 and s.aureus atcc 29213. CCL20 gene transcription is activated by H. pylori, which activates NF-kappaB through intracellular signal pathway which involves IkappaB kinase and NF-kappaB-inducing kinase. MIP-3 alpha is invloved in chemokine-mediated lymphocyte trafficking during gastric inflammation in Helicobacter infection. CCL20 expression is involved in the recruitment of CD45R0-positive T cell subsets into the intestinal lamina propria.
MIP-3A is in charge of the advancement of pulpal inflammation through the recruitment of C-C motif Receptor 6-expressing lymphocytes Vaginal epithelial cells respond to factors present in semen by secreting MIP-3 alpha, which increases langerhans cells recruitment during HIV transmission.
Synonyms
Small inducible cytokine A20 precursor, CCL20, Macrophage inflammatory protein 3 alpha, MIP-3-alpha, Liver and activation- regulated chemokine, CC chemokine LARC, Beta chemokine exodus-1, CKb4, LARC, ST38, MIP3A, MIP-3a, SCYA20, C-C motif chemokine 20, CC chemokine ST38, exodus-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MIP-3a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL-20 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 MIP-3a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ASNYDCCLSY IQTPLPSRAI VGFTRQMADE ACDINAIIFH TKKRKSVCAD PKQNWVKRAV NLLSLRVKKM.
Background
What is the molecular weight/Mw of CCL20 MOUSE Protein?
CCL20 MOUSE Protein has a total Mw of 7.9kDa.

What is the source or expression system of CCL20 MOUSE Protein?
Escherichia Coli.

What is the Purity of CCL20 MOUSE Protein?
CCL20 MOUSE Protein is > 95% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL20 MOUSE Protein?
The Activity is calculated by its ability to chemoattract primary human T cells at 2-20ng/ml, corresponding to a specific activity of 50,000-500,000 units/mg.

What is the amino acid sequence of CCL20 MOUSE Protein?
ASNYDCCLSY IQTPLPSRAI VGFTRQMADE ACDINAIIFH TKKRKSVCAD PKQNWVKRAV NLLSLRVKKM.

What applications can CCL20 MOUSE Protein be used in?
CCL20 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL20 MOUSE Protein?
The endotoxin level is minimal, CCL20 MOUSE Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL20 MOUSE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CCL20 MOUSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

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