Search: 1000 results found for "Selectin"

Description:

Vascular Endothelial Growth Factor receptor-1 Human Recombinant, HEK Active

FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

Product # :

PKA-134

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Description

FLT1 Human Recombinant is a single, glycosylated polypeptide chain containing 535 amino acids (27-328a.a) and having a molecular mass of 60.3kDa (calculated). FLT1 is fused to a 233 amino acid hIgG-Tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293

Formulation

FLT1 protein solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The ED50 range ≤ 60ng/ml and is measured by its ability to inhibit proliferation using HUVEC human umbilical vein endothelial cells in the
presence of Human VEGF165.

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Synonyms
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
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.Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
SKLKDPELSL KGTQHIMQAG QTLHLQCRGE AAHKWSLPEM VSKESERLSI TKSACGRNGK QFCSTLTLNT AQANHTGFYS CKYLAVPTSK KKETESAIYI FISDTGRPFV EMYSEIPEII HMTEGRELVI PCRVTSPNIT VTLKKFPLDT LIPDGKRIIW DSRKGFIISN ATYKEIGLLT CEATVNGHLY KTNYLTHRQT NTIIDVQIST PRPVKLLRGH TLVLNCTATT PLNTRVQMTW SYPDEKNKRA SVRRRIDQSN SHANIFYSVL TIDKMQNKDK GLYTCRVRSG PSFKSVNTSV HILEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGK.
Background
VEGFR-1 (Vascular Endothelial Growth Factor Receptor-1), also known as Flt-1 (Fms-like tyrosine kinase 1), is a critical receptor involved in angiogenesis and vascular development. This research paper delves into the structure, function, and therapeutic implications of VEGFR-1, shedding light on its multifaceted role in various physiological and pathological processes.
VEGFR-1 is a transmembrane receptor tyrosine kinase belonging to the VEGF receptor family. It is primarily expressed on endothelial cells and plays a pivotal role in mediating the cellular responses to VEGF ligands. Upon ligand binding, VEGFR-1 initiates intracellular signaling cascades that regulate endothelial cell proliferation, migration, and survival, ultimately contributing to the formation of new blood vessels.
The structure of VEGFR-1 comprises distinct domains, including an extracellular ligand-binding domain, a transmembrane domain, and an intracellular tyrosine kinase domain. The extracellular domain facilitates the interaction between VEGF ligands and the receptor, while the intracellular domain transduces downstream signals by phosphorylating specific tyrosine residues.
VEGFR-1 exhibits not only ligand-dependent but also ligand-independent functions. In addition to its role as a VEGF receptor, it can act as a decoy receptor, sequestering VEGF and modulating the bioavailability of VEGF ligands. This unique property allows VEGFR-1 to regulate VEGF signaling and influence angiogenic processes.
The signaling pathways activated by VEGFR-1 are diverse and intricate, involving multiple downstream effectors, such as PI3K/AKT, MAPK/ERK, and STAT proteins. These pathways regulate endothelial cell behaviors, including proliferation, migration, and differentiation, which are crucial for angiogenesis. Perturbations in VEGFR-1 signaling have been implicated in various pathological conditions, including cancer, retinopathy, and inflammatory disorders.
The therapeutic targeting of VEGFR-1 has gained considerable attention for its potential in managing angiogenesis-related diseases. Inhibitors specifically designed to block VEGFR-1 have been developed to suppress aberrant angiogenesis and impede tumor growth. Moreover, VEGFR-1-based therapies have been explored for ocular diseases like wet age-related macular degeneration (AMD) and diabetic retinopathy, aiming to alleviate pathological neovascularization.
The availability of VEGFR-1 human recombinant proteins has facilitated in-depth research and the development of potential therapeutic interventions. Recombinant VEGFR-1 proteins serve as valuable tools for investigating VEGF-VEGFR-1 interactions, screening drug candidates, and elucidating the underlying molecular mechanisms of VEGFR-1-mediated signaling pathways.

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:

Desmin Chicken Gizzard

Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.

Product # :

PRO-2783

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Description

Desmin Chicken having a calculated molecular mass of 53 kDa, pI-5.4.

Source

Chicken gizzard.

Formulation

Desmin was lyophilized from a 1mg/ml solution containing 10 mM sodium phosphate buffer pH 7.5, 6M urea, 1mM EDTA, 2mM DTT and 10mM methylammonium chloride.

Purity

Greater than 98.0% as determined by SDS-PAGE.

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Synonyms
Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Store the lyophilized Desmin between 2-8°C, do not freeze. Upon reconstitution Desmin should be stored at -20°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Desmin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
Desmin, an intermediate filament protein, plays a fundamental role in maintaining the structural integrity and function of muscle cells. While extensive research has been conducted on desmin in mammals, the study of desmin in chickens is an emerging area with considerable potential for advancing our understanding of muscle biology. Chickens are valuable model organisms for studying muscle development, growth, and regeneration due to their relatively simple muscular system and economic significance in poultry production. This research aims to provide a comprehensive exploration of desmin in chickens, shedding light on its functions and implications for muscle structure and function.
The primary objective of this research is to elucidate the role of desmin in chicken muscle structure and development. In vitro and in vivo experiments, utilizing chicken cell cultures and embryonic models, will be conducted to investigate how desmin contributes to the organization of muscle fibers, sarcomere assembly, and myofibrillogenesis. Understanding these mechanisms is fundamental for deciphering the complexities of muscle development in chickens.
The second objective is to assess the clinical and economic relevance of desmin in poultry production. Studies involving broiler chickens will be conducted to evaluate the impact of desmin mutations or variations on muscle growth, meat quality, and disease susceptibility. These investigations may provide valuable insights into potential strategies for enhancing poultry production efficiency and meat quality.
The third objective is to explore the potential applications of desmin in biotechnology and tissue engineering. Research will investigate the use of desmin-expressing chicken cells as models for studying muscle-related diseases and for developing tissue engineering approaches for muscle repair and regeneration.
By delving into the functions and roles of desmin in chickens, this research aims to expand our knowledge of muscle biology, its implications for poultry production, and its potential applications in biotechnology and regenerative medicine.

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:

GRO/KC (CXCL1) Mouse Recombinant, His Tag

Growth-regulated alpha protein, CXCL1, Platelet-derived growth factor-inducible protein KC, Secretory protein N51, KC, Fsp, N51, gro, Gro1, Mgsa, Scyb1, chemokine (C-X-C motif) ligand 1.

Product # :

CHM-002

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SDS-PAGE

Description

GRO1/KC Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 97 amino acids (25-96 a.a.) and having a molecular mass of 10.5kDa.GRO1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GRO1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.1M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Chemokine (C-X-C motif) ligand 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). It is secreted by human melanoma cells, has mitogenic properties and is implicated in melanoma pathogenesis. CXCL1 is expressed by macrophages, neutrophils and epithelial cells, and has neutrophil chemoattractant activity. CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis. This chemokine elicits its effects by signaling through the chemokine receptor CXCR2. The gene for CXCL1 is located on human chromosome 4 amongst genes for other CXC chemokines.
Synonyms
Growth-regulated alpha protein, CXCL1, Platelet-derived growth factor-inducible protein KC, Secretory protein N51, KC, Fsp, N51, gro, Gro1, Mgsa, Scyb1, chemokine (C-X-C motif) ligand 1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAPIAN ELRCQCLQTM AGIHLKNIQS LKVLPSGPHC TQTEVIATLK NGREACLDPE APLVQKIVQK MLKGVPK.
Background
What is the molecular weight/Mw of CXCL1 MOUSE, HIS Protein?
CXCL1 MOUSE, HIS Protein has a total Mw of 10.5kDa.

What is the source or expression system of CXCL1 MOUSE, HIS Protein?
Escherichia Coli.

What is the Purity of CXCL1 MOUSE, HIS Protein?
CXCL1 MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL1 MOUSE, HIS Protein?
The biological functionality of CXCL1 MOUSE, HIS Protein will be determined in the future.

What is the amino acid sequence of CXCL1 MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMAPIAN ELRCQCLQTM AGIHLKNIQS LKVLPSGPHC TQTEVIATLK NGREACLDPE APLVQKIVQK MLKGVPK.

What applications can CXCL1 MOUSE, HIS Protein be used in?
CXCL1 MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL1 MOUSE, HIS Protein?
The endotoxin level is minimal, CXCL1 MOUSE, HIS 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:

MORC Family CW-Type Zinc Finger 3 Human Recombinant

MORC family CW-type zinc finger protein 3, Nuclear matrix protein 2, Zinc finger CW-type coiled-coil domain protein 3, MORC3, KIAA0136, NXP2, ZCWCC3.

Product # :

PRO-2674

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Description

Recombinant Human MORC Family CW-Type Zinc Finger 3 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 122kDa. MORC3 is expressed with a 10xHis tag and purified by proprietary chromatographic techniques.

Source

Sf9 insect cells.

Formulation

MORC3 is supplied in 20mM Sodium phosphate, pH 7.6, 500mM NaCl and 20% glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
MORC Family CW-Type Zinc Finger 3 (MORC3) localizes to the nuclear matrix. MORC3 takes part in the regulation of the tumor suppressor protein p53. MORC3may indicate on dermatomyositis (DM) as autoantibodies against this protein have been found in patients.
Synonyms
MORC family CW-type zinc finger protein 3, Nuclear matrix protein 2, Zinc finger CW-type coiled-coil domain protein 3, MORC3, KIAA0136, NXP2, ZCWCC3.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
Immunological Functions
1. Binds IgG-type human auto-antibodies.2. immunodot test with positive/negative samples.
Applications
Western blot with patient sample.

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:

Allergenic Isoflavone Reductase-Like Protein Bet v 6.0102 Recombinant

Allergenic isoflavone reductase-like protein Bet v 6.0102, BETV6.0102.

Product # :

ALR-018

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Description

Recombinant BETV6.0102 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 36,636 Dalton. BETV6.0102 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Sf9 insect cells.

Formulation

BETV6.0102 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
BETV6.0102 allergen is one of Isoflavone reductases which were found in pear, orange, apple, mango, lychee and other plants. Isoflavone reductases are plant defense proteins which induced by plant stress, e.g. high salinity, freeze or drought.
Synonyms
Allergenic isoflavone reductase-like protein Bet v 6.0102, BETV6.0102.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

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-22 Mouse Recombinant, Pegylated

IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.

Product # :

CYT-701

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Description

Pegylated Interleukin-22 Mouse Recombinant produced in E.Coli is a single, non-glycosylated homodimeric polypeptide chain containing 147 amino acids and an aditional Ala amino acid at N-terminus having a molecular mass of 36 kDa as determioned by mass spectometry. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as a 50 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. The Murine IL-22 is Mono-pegylated (with 20 kDa PEG) purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated solution at 0.65mg/ml containing 0.003mM NaHCO3.

Purity

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

Biological Activity

The ED50 as determined by STAT3 phosphorylation assay in HepG cells. The activity in vitro was found to be ~ 10% compared to the non-pegylated mouse IL22.

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Introduction
Interleukin-22 (IL-22), also known as IL-10-related T cell-derived inducible factor (IL-TIF) was initially identified as a gene induced by IL-9 in mouse T cells and mast cells. Mouse IL-22 cDNA encodes a 179 amino acid residue protein with a putative 33 amino acids signal peptide that is cleaved to generate a 147 aa mature protein that shares approximately 79% and 22% aa sequence identity with human IL-22 and IL-10, respectively. IL-22 has been shown to activate STAT-1 and STAT-3 in several hepatoma cell lines and upregulate the production of acute phase proteins. IL-22 is produced by normal mouse T cells upon Con A activation. Mouse IL-22 expression is also induced in various organs upon lipopolysaccharide injection, suggesting that IL-22 may be involved in inflammatory responses. The functional IL-22 receptor complex consists of two receptor subunits, IL-22R (previously an orphan receptor named CRF2-9) and IL-10Rβ (previously known as CRF2-4), belonging to the class II cytokine recep
Synonyms
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized pegylated murine IL22 although stable at room temperature for several days, should be stored desiccated below -20°C. Upon reconstitution at 0.1mg/ml pegylated mouse IL22 and up to 2mg/ml, filter and sterilized, the protein can be stored at 4 degrees Celsius for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized pegylated mouse Interleukin -22 in sterile 0.4% NaHCO3 adjusted to pH 8-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

Description:

Interleukin-12 p40 Human Recombinant

NKSF2, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 40 kDa subunit (CLMF p40), TSF, Edodekin-alpha, IL-12 p40, IL-12B, IL-12 subunit p40, NK cell stimulatory factor chain 2.

Product # :

CYT-488

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Description

Interleukin-12 p40 His Human Recombinant produced in E.Coli is single, a non-glycosylated, polypeptide chain containing 306 amino acids fragment (23-328) with an amino-terminal hexahistidine tag. The IL-12 p40 His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin-12 p40 His is supplied in 1xPBS and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Active IL-12 is a p70 disulphide-linked dimer composed of p35 and p40 subunits. The protein is a pleiotropic cytokine produced primarily by antigen presenting cells and has multiple effects on T lymphocytes and natural killer cells in terms of stimulating cytotoxicity, proliferation, production of other cytokines and Th1 subset differentiation.
Synonyms
NKSF2, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 40 kDa subunit (CLMF p40), TSF, Edodekin-alpha, IL-12 p40, IL-12B, IL-12 subunit p40, NK cell stimulatory factor chain 2.
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.

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:

Epithelial Cell Adhesion Molecule Human Recombinant, Sf9

Epithelial Cell Adhesion Molecule , Tumor-Associated Calcium Signal Transducer 1, Major Gastrointestinal Tumor-Associated Protein GA733-2, Adenocarcinoma-Associated Antigen, Cell Surface Glycoprotein Trop-1, Epithelial Glycoprotein 314, TACSTD1, EGP314, MIC18, TROP1, M4S1, KSA, Membrane Component, Chromosome 4, Surface Marker (35kD Glycoprotein), Antigen Identified By Monoclonal Antibody AUA1, Human Epithelial Glycoprotein-2, Epithelial Cell Surface Antigen, Epithelial Glycoprotein, KS 1/4 Antigen, CD326 Antigen, GA733-2, HEGP314, HNPCC8, Ep-CAM, DIAR5, EGP-2, EGP40, KS1/4, MK-1, M1S2, ESA, EGP, EPCAM.

Product # :

PRO-2238

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Description

EPCAM produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (24-265 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 248 amino acids and having a molecular mass of 28.2kDa.EPCAM shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

EPCAM protein solution (1mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
EPCAM is a carcinoma-associated antigen and belongs to a family which includes at least 2 type I membrane proteins. The EPCAM protein has a role in embryonic stem cells proliferation and differentiation. EPCAM is used as a target for immunotherapy treatment of human carcinomas. EPCAM is expressed on most normal epithelial cells and gastrointestinal carcinomas and acts as a homotypic calcium-independent cell adhesion molecule. Epithelial cell adhesion molecules (EPCAM) can act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for supplying immunological barrier as a first line of defense against mucosal infection. EPCAM gene mutations result in congenital tufting enteropathy.
Synonyms
Epithelial Cell Adhesion Molecule , Tumor-Associated Calcium Signal Transducer 1, Major Gastrointestinal Tumor-Associated Protein GA733-2, Adenocarcinoma-Associated Antigen, Cell Surface Glycoprotein Trop-1, Epithelial Glycoprotein 314, TACSTD1, EGP314, MIC18, TROP1, M4S1, KSA, Membrane Component, Chromosome 4, Surface Marker (35kD Glycoprotein), Antigen Identified By Monoclonal Antibody AUA1, Human Epithelial Glycoprotein-2, Epithelial Cell Surface Antigen, Epithelial Glycoprotein, KS 1/4 Antigen, CD326 Antigen, GA733-2, HEGP314, HNPCC8, Ep-CAM, DIAR5, EGP-2, EGP40, KS1/4, MK-1, M1S2, ESA, EGP, EPCAM.
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
QEECVCENYK LAVNCFVNNN RQCQCTSVGA QNTVICSKLA AKCLVMKAEM NGSKLGRRAK PEGALQNNDG LYDPDCDESG LFKAKQCNGT STCWCVNTAG VRRTDKDTEI TCSERVRTYW IIIELKHKAR EKPYDSKSLR TALQKEITTR YQLDPKFITS ILYENNVITI DLVQNSSQKT QNDVDIADVA YYFEKDVKGE SLFHSKKMDL TVNGEQLDLD PGQTLIYYVD EKAPEFSMQG LKHHHHHH

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-33 Human Recombinant

Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, NFEHEV, DKFZp586H0523, RP11-575C20.2, IL-33.

Product # :

CYT-425

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Shipped at Room temp

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Description

Interleukin33 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids and having a molecular mass of 18,125 Dalton. The IL-33 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from 10mM NaP pH-7.5.

Purity

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

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Introduction
Interleukin 33 (IL-33) is a 32kDa proinflammatory cytokine that may also regulate gene transcription in producer cells. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1 (IL1 receptor-like-1), which is known also as ST2. Binding of IL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces expression of IL-4, IL-5, IL-13 and leads to severe pathological changes in mucosal organs and in vitro, it can be divided to N-terminal fragment of 12kDa and C-terminal fragment of 18kDa by cleavage of caspase-1.
Synonyms
Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, NFEHEV, DKFZp586H0523, RP11-575C20.2, IL-33.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-33 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL33 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 IL-33 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSITGISPIT EYLASLSTYN DQSITFALED ESYEIYVEDL KKDEKKDKVL LSYYESQHPS NESGDGVDGK MLMVTLSPTK DFWLHANNKE HSVELHKCEK PLPDQAFFVL HNMHSNCVSF ECKTDPGVFI GVKDNHLALI KVDSSENLCT ENILFKLSET.

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:

Platelet Endothelial Cell Adhesion Molecule 1 Human Recombinant

Platelet endothelial cell adhesion molecule, PECAM1, CD31, CD31/EndoCAM, endoCAM, GPIIA', PECA1, PECAM-1, Platelet Endothelial Cell Adhesion Molecule 1.

Product # :

CYT-924

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Description

PECAM1 Human Recombinant produced in Sf9 Baculovirus is a single, non-glycosylated polypeptide chain containing 582 amino acids (28-601a.a.) and having a molecular mass of 65.5kDa (Migrates at 70-100kDa on SDS-PAGE under reducing conditions).PECAM1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

PECAM1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Platelet endothelial cell adhesion molecule (PECAM1) induces susceptibility to atherosclerosis. PECAM1 averts phagocyte ingestion of closely apposed viable cells by transmitting detachment signals, and transforms function upon apoptosis, thus promoting tethering of dying cells to phagocytes. The encounter of a viable cell with a phagocyte via the homophilic interaction of PECAM1 on both cell surfaces as a result causing the viable cell's active repulsion from the phagocyte.
Synonyms
Platelet endothelial cell adhesion molecule, PECAM1, CD31, CD31/EndoCAM, endoCAM, GPIIA', PECA1, PECAM-1, Platelet Endothelial Cell Adhesion Molecule 1.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
QENSFTINSV DMKSLPDWTV QNGKNLTLQC FADVSTTSHV KPQHQMLFYK DDVLFYNISS MKSTESYFIP EVRIYDSGTY KCTVIVNNKE KTTAEYQVLV EGVPSPRVTL DKKEAIQGGI VRVNCSVPEE KAPIHFTIEK LELNEKMVKL KREKNSRDQN FVILEFPVEE QDRVLSFRCQ ARIISGIHMQ TSESTKSELV TVTESFSTPK FHISPTGMIM EGAQLHIKCT IQVTHLAQEF PEIIIQKDKA IVAHNRHGNK AVYSVMAMVE HSGNYTCKVE SSRISKVSSI VVNITELFSK PELESSFTHL DQGERLNLSC SIPGAPPANF TIQKEDTIVS QTQDFTKIAS KSDSGTYICT AGIDKVVKKS NTVQIVVCEM LSQPRISYDA QFEVIKGQTI EVRCESISGT LPISYQLLKT SKVLENSTKN SNDPAVFKDN PTEDVEYQCV ADNCHSHAKM LSEVLRVKVI APVDEVQISI LSSKVVESGE DIVLQCAVNE GSGPITYKFY REKEGKPFYQ MTSNATQAFW TKQKASKEQE GEYYCTAFNR ANHASSVPRS KILTVRVILA PWKKVEHHHH HH.

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

Description:

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:

Cytokeratin 14 Human Recombinant

Keratin, type I cytoskeletal 14, Cytokeratin-14, CK-14, Keratin-14, K14, KRT14, NFJ, CK14, EBS3, EBS4.

Product # :

PRO-348

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Description

Cytokeratin 14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 51,530 Dalton. The KRT14 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (1mg/ml) was lyophilized after from a sterile solution containing 30mM Tris-HCl pH-8, 9.5M urea, 2mM DTT, 2mM EDTA and 10mM methylammonium chloride.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Cytokeratin 14 is a member of the keratin family, the most diverse group of intermediate filaments. Cytokeratin 14 is a type I keratin, is usually found as a heterotetramer with two keratin 5 molecules, a type II keratin. Together they form the cytoskeleton of epithelial cells. Mutations in the genes for these keratins are associated with epidermolysis bullosa simplex. At least one pseudogene has been identified at 17p12-p11.
Synonyms
Keratin, type I cytoskeletal 14, Cytokeratin-14, CK-14, Keratin-14, K14, KRT14, NFJ, CK14, EBS3, EBS4.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized KRT14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution KRT14 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 CK-14 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Reconstitution to filaments
Performed by mixing equimolar amounts of cytokeratins of type I and type II at concentrations of approx. 0.5 mg/ml, both dissolved in 9.5M urea buffer (see above). Protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4M urea and then to low salt condition (50mM NaCI, 2mM dithiothreitol, 10mM Tris-HCI, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco's PBS).

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:

s100bb Human homodimer

Product # :

PRO-2797

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Description

s100bb Human produced in Human brain tissue is suitable for use as a standard in immunoassay and as an immunogen for antiserum production.

Source

Human brain tissue.

Formulation

s100bb was lyophilized from 5mM Tris-HCl, pH 7.5, 2mM EDTA and 5mM 2-mercaptoethanol.

Purity

Greater than 95.0% .

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized s100bb homodimer although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution s100bb 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 s100bb in sterile 18MΩ-cm H2O containing 5mM 2- mercaptoethanol not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
S100BB is not only active in mature brains but also plays a significant role during brain development. It contributes to neural progenitor cell proliferation, neuronal migration, and differentiation. Studies have suggested that alterations in S100BB expression during development might influence the wiring of neural circuits, potentially impacting cognitive functions later in life. Investigating these developmental aspects of S100BB provides essential insights into neurogenesis and brain architecture.
Implications in Neurological Disorders:
Research has indicated potential links between abnormal S100BB levels and neurological disorders. Elevated S100BB levels have been observed in conditions such as traumatic brain injury, stroke, and neurodegenerative diseases. Its release into the bloodstream following CNS damage has positioned S100BB as a biomarker for CNS injury. Additionally, studies have explored its involvement in neuroinflammation and synaptic dysfunction, offering a glimpse into its role in diseases like Alzheimer’s and Parkinson’s.
Conclusion:
S100BB, once regarded as a brain-specific protein, has emerged as a pivotal player in neurological signaling and development. Its intricate involvement in cellular processes within the CNS underscores its significance in understanding brain function and disorders. As research delves deeper into the regulatory mechanisms and functional implications of S100BB, it holds promise for unveiling novel therapeutic targets for neurological diseases. This study aims to shed light on the multifaceted nature of S100BB, emphasizing its crucial roles in the intricate landscape of the central nervous system.

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:

Human Serum Albumin Recombinant, Plant

Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.

Product # :

PRO-595

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Description

HSA Human Recombinant produced in Plant is a non-glycosylated, polypeptide chain containing 585 amino acids and having a molecular mass of 67 kDa. The optimum concentration for recombinant Albumin to be used in cell culture ranges between 0.5gr to 2gr per liter. The recombinant Albumin is purified by proprietary chromatographic techniques.

Source

Rice Grain.

Formulation

The Recombinant Albumin was lyophilized with sodium chloride. A 10% w/v solution when dissolved in water will contain 50mM NaCl.

Purity

Greater than 98% as determined by SDS-PAGE.

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Introduction
Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin. Albumin is a soluble, monomeric protein which comprises about one-half of the blood serum protein. Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. Albumin is a globular unglycosylated serum protein of molecular weight 65,000. The human albumin gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
HSA is widely used to stabilize blood volume generally from donors but the fear of contamination such as HIV & Hepatitis has enticed great interest in the recombinant form which is identical to the natural blood.
Synonyms
Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
Physical Appearance
Sterile Filtered white lyophilized powder.
Stability
Recombinant Albumin although stable at 4°C for 3 weeks, should be stored at -18°C.Please prevent freeze-thaw cycles.
Applications
Recombinant Albumin can be used as a media culture supplement at concentrations up to 5 grams per liter. Gradual adaptation of cell lines over several passages to a concentration of 0.5gr to 2gr per liter.

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

Description:

Complement Factor B Human

CFB, C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, BF, BFD, AHUS4, ARMD14, CFAB, CFBD, FB, FBI12, GBG, H2-Bf.

Product # :

PRO-2698

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Description

Human Complement Factor B produced in Human plasma is glycosylated polypeptide chain having a total molecular mass of 93kDa.

Source

Human Plasma.

Formulation

CFB protein solution contains 10mM Sodium phosphate and 145mM NaCl, pH 7.2.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Complement Factor B, also known as CFB, encodes complement factor B which is a component of the alternative pathway of complement activation. Factor B circulates in the blood as a single chain polypeptide. Once the alternative pathway is activated it is cleaved by complement factor D yielding the noncatalytic chain Ba and the catalytic subunit Bb. The active subunit Bb is a serine protease which connects with C3b to form the alternative pathway C3 convertase. Also, Bb is involved in the proliferation of preactivated B lymphocytes, while Ba inhibits their proliferation.
Synonyms
CFB, C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, BF, BFD, AHUS4, ARMD14, CFAB, CFBD, FB, FBI12, GBG, H2-Bf.
Physical Appearance
Sterile filtered solution.
Stability
CFB Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.

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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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.

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:

BCA-1/BLC Mouse Recombinant (CXCL13)

C-X-C motif chemokine 13, B lymphocyte chemoattractant, CXC chemokine BLC, Small-inducible cytokine B13, Cxcl13, Blc, Scyb13.

Product # :

CHM-030

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Description

CXCL13 Mouse Recombinant (22-109) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 88 amino acids and having a molecular mass of 10kDa.The BCA-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The BCA1 protein was lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as measured by its ability to chemoattract human CXCR5-transfected mouse BaF3 cells, is less than 2µg/ml.

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Introduction
BCA-1 is a CXC chemokine that is highly expressed in thesecondary lymphoid organs, such as follicles of the spleen, lymph nodes, and Peyer's patches. CXCL13 promotes the migration of B lymphocytes (compared to T cells and macrophages), by stimulating calcium influx into, and chemotaxis of, cells expressing Burkitt's lymphoma receptor 1 (BLR1). BCA1 therefore function in the homing of B lymphocytes to follicles. Human BCA-1 shares a 64% amino acid sequence similarity with the mouse protein and 23 - 34% amino acid sequence identity with other known CXC chemokines. Recombinant or chemically synthesized BCA1 is a potent chemoattractant for B lymphocytes but not T lymphocytes, monocytes or neutrophils. BLR1, a G protein-coupled receptor originally isolated from Burkitt’s lymphoma cells, has now been shown to be the specific receptor for BCA1. Among cells of the hematopoietic lineages, the expression of BLR-1, now designated CXCR-5, is restricted to B lymphocytes and a subpopulation of T helper memory cells.
Synonyms
C-X-C motif chemokine 13, B lymphocyte chemoattractant, CXC chemokine BLC, Small-inducible cytokine B13, Cxcl13, Blc, Scyb13.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BCA1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BCA1 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 CXCL13 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ILEAHYTNLK CRCSGVISTV VGLNIIDRIQ VTPPGNGCPK TEVVIWTKMK KVICVNPRAK WLQRLLRHVQ SKSLSSTPQA PVSKRRAA.
Background
What is the molecular weight/Mw of CXCL13 MOUSE Protein?
CXCL13 MOUSE Protein has a total Mw of 10kDa.

What is the source or expression system of CXCL13 MOUSE Protein?
Escherichia Coli.

What is the Purity of CXCL13 MOUSE Protein?
CXCL13 MOUSE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL13 MOUSE Protein?
The ED50, as measured by its ability to chemoattract human CXCR5-transfected mouse BaF3 cells, is less than 2µg/ml.

What is the amino acid sequence of CXCL13 MOUSE Protein?
ILEAHYTNLK CRCSGVISTV VGLNIIDRIQ VTPPGNGCPK TEVVIWTKMK KVICVNPRAK WLQRLLRHVQ SKSLSSTPQA PVSKRRAA.

What applications can CXCL13 MOUSE Protein be used in?
CXCL13 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL13 MOUSE Protein?
The endotoxin level is minimal, CXCL13 MOUSE Protein was purified using conventional chromatography techniques.

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

Description:

Beta Defensin-1 Human Recombinant

Beta-defensin 1, BD-1, Defensin beta 1, hBD-1, HBD1, HBP1, DEFB1, HBD-1, HBP-1, DEFB101, DEFB-1, MGC51822.

Product # :

CYT-564

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Description

Beta Defensin-1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 47 amino acids and having a molecular mass of 5 kDa.The BD-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Human BD-1 was lyophilized from a concentrated (1mg/ml) solution containing 20mM PBS pH-7.4 and 130mM sodium chloride.

Purity

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

Biological Activity

Determined by its ability to chemoattract CD34+ dendritic cells using a concentration range of 100-1000ng/ml corresponding to a specific activity of 1,000-10,000IU/mg.

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Synonyms
Beta-defensin 1, BD-1, Defensin beta 1, hBD-1, HBD1, HBP1, DEFB1, HBD-1, HBP-1, DEFB101, DEFB-1, MGC51822.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Beta Defensin-1 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-1 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Beta Defensin-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GNFLTGLGHR SDHYNCVSSG GQCLYSACPI FTKIQGTCYR GKAKCCK.
Background
Beta Defensin-1 Human Recombinant: Unveiling its Potential in Innate Immunity and Therapeutic Applications
Abstract:

Beta Defensin-1 (BD-1), a member of the defensin family, plays a crucial role in innate immunity and host defense. This research paper provides an overview of BD-1 human recombinant, exploring its molecular characteristics, antimicrobial properties, and therapeutic applications. Understanding the multifaceted role of BD-1 offers new avenues for developing innovative immunotherapies. This article offers a concise analysis of BD-1, highlighting its impact on innate immunity and its therapeutic potential.
Introduction:

Innate immunity serves as the first line of defense against invading pathogens. BD-1, a key peptide within the defensin family, exhibits broad-spectrum antimicrobial activity and plays a pivotal role in host defense mechanisms. This paper provides an overview of BD-1, shedding light on its structure, function, and therapeutic potential.
BD-1 Structure and Function:

BD-1 is a cationic peptide with a conserved cysteine motif that confers its antimicrobial properties. It acts by disrupting the integrity of microbial cell membranes, leading to microbial death. Additionally, BD-1 exhibits immunomodulatory effects by stimulating immune cell recruitment and cytokine production.
Antimicrobial Properties and Therapeutic Applications:

BD-1 demonstrates antimicrobial activity against a wide range of pathogens, including bacteria, fungi, and viruses. Its ability to combat multidrug-resistant strains makes it an attractive candidate for the development of novel antimicrobial therapies. Furthermore, BD-1's immunomodulatory effects contribute to its potential in treating inflammatory and infectious diseases.
Therapeutic Potential of BD-1 Human Recombinant:

BD-1 human recombinant holds significant promise in the field of immunotherapy. Strategies aimed at enhancing BD-1 expression or delivering exogenous BD-1 may help boost innate immune responses in patients with compromised immune systems or chronic infections. Furthermore, BD-1-based therapeutics could be developed to combat antibiotic-resistant infections and prevent biofilm formation.
Challenges and Future Directions:

While BD-1 shows immense therapeutic potential, challenges must be addressed. Further research is necessary to optimize the delivery methods of BD-1 and evaluate its long-term safety and efficacy. Additionally, understanding the interplay between BD-1 and other immune factors will aid in developing combinatorial approaches for enhanced therapeutic outcomes.
Conclusion:

BD-1 human recombinant represents a promising avenue for developing novel immunotherapies and combating antimicrobial resistance. Understanding the molecular mechanisms and functional implications of BD-1 in innate immunity opens new horizons for innovative treatments. Continued research in this field has the potential to revolutionize the field of immunotherapy and improve patient outcomes.
What is the molecular weight/Mw of BD1 Protein?
BD1 Protein has a total Mw of 5kDa.

What is the source or expression system of BD1 Protein?
Escherichia Coli.

What is the Purity of BD1 Protein?
BD1 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of BD1 Protein?
Determined by its ability to chemoattract CD34+ dendritic cells using a concentration range of 100-1000ng/ml corresponding to a specific activity of 1,000-10,000IU/mg.

What is the amino acid sequence of BD1 Protein?
GNFLTGLGHR SDHYNCVSSG GQCLYSACPI FTKIQGTCYR GKAKCCK.

What applications can BD1 Protein be used in?
BD1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BD1 Protein?
The endotoxin level is minimal, BD1 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:

Interleukin-1 Receptor Antagonist Rat Recombinant, His Tag

Interleukin-1 receptor antagonist protein, IL-1RN, IL-1ra, IRAP, IL1 inhibitor, Il1rn, Il-1ra, Interleukin-1 Receptor Antagonist, IL-1ra, IL 1RA.

Product # :

CYT-899

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Description

IL 1RA Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids (27-178a.a.) and having a molecular mass of 19.8kDa.IL 1RA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL 1RA protein solution (1mg/ml) containing Phosphate Buffer Saline (pH7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by analysis by SDS-PAGE.

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Introduction
Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.
Synonyms
Interleukin-1 receptor antagonist protein, IL-1RN, IL-1ra, IRAP, IL1 inhibitor, Il1rn, Il-1ra, Interleukin-1 Receptor Antagonist, IL-1ra, IL 1RA.
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 MGSHPAGKRP CKMQAFRIWD TNQKTFYLRN NQLIAGYLQG PNTKLEEKID MVPIDFRNVF LGIHGGKLCL SCVKSGDDTK LQLEEVNITD LNKNKEEDKR FTFIRSETGP TTSFESLACP GWFLCTTLEA DHPVSLTNTP KEPCTVTKFY FQEDQ.

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:

Persephin Human Recombinant

Persephin, PSP, PSPN.

Product # :

CYT-801

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Description

PSPN Human Recombinant produced in E.Coli is a disulfide-linked homodimer containing 2x96 amino acids and having a molecular mass of 20.5kDa. The PSPN is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using human TT medullary thyroid cancer cells is less than 10ng/ml, corresponding to a specific activity of > 1.0 × 100,000 IU/mg.

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Introduction
Persephin is a member of the GDNF ligand subfamily of the TGF-beta superfamily. PSPN encourages the existence and growth of key dopaminergic and motor neurons, as well as taking part in kidney development. Nonetheless, persephin does not support existence of peripheral neurons.
Synonyms
Persephin, PSP, PSPN.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PSPN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PSPN 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 PSPN in 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ALSGPCQLWS LTLSVAELGL GYASEEKVIF RYCAGSCPRG ARTQHGLALA RLQGQGRAHG GPCCRPTRYT DVAFLDDRHR WQRLPQLSAA ACGCGG.

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:

Secreted Protein Acidic & Rich in Cysteine Recombinant Human

Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine.

Product # :

PRO-2602

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Description

Secreted Protein Acidic & Rich in Cysteine Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 286 amino acids and having a molecular mass of 32.7kDa.SPARC is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 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 the cell growth of Mv1Lu mink lung epithelial cells is < 3.0 µg/mL, corresponding to a specific activity of > 333 IU/mg.

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Introduction
SPARC, an acronym for “secreted protein, acidic and rich in cysteine”, is also known as osteonectin or BM-40. It is the founding member of a family of secreted matricellular proteins with similar domain structure. The 303 amino acid, 43 kDa protein contains a 17 aa signal sequence, an N-terminal acidic region that binds calcium, a follistatin domain containing Kazal-like sequences, and a C-terminal extracellular calcium (EC) binding domain with two EF-hand motifs. SPARC is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, especially in areas of tissue morphogenesis and remodeling. SPARC shows context-specific effects, but generally inhibits adhesion, spreading and proliferation, and promotes collagen matrix formation. For endothelial cells, SPARC disrupts focal adhesions and binds and sequesters PDGF and VEGF. SPARC is abundantly expressed in bone, where it promotes osteoblast differentiation and inhibits adipogenesis.
Synonyms
Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SPARC although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Secreted Protein Acidic & Rich in Cysteine should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized SPARC in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APQQEALPDE TEVVEETVAE VTEVSVGANP VQVEVGEFDD GAEETEEEVV AENPCQNHHC KHGKVCELDE NNTPMCVCQD PTSCPAPIGE FEKVCSNDNK TFDSSCHFFA TKCTLEGTKK GHKLHLDYIG PCKYIPPCLD SELTEFPLRM RDWLKNVLVT LYERDEDNNL LTEKQKLRVK KIHENEKRLE AGDHPVELLA RDFEKNYNMY IFPVHWQFGQ LDQHPIDGYL SHTELAPLRA PLIPMEHCTT RFFETCDLDN DKYIALDEWA GCFGIKQKDI DKDLVI.

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-33 Mouse Recombinant

Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, Il-33, Il1f11, 9230117N10Rik, Il33.

Product # :

CYT-655

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Description

Interleukin33 Mouse recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 159 amino acids and having a molecular mass of 17.7 kDa.

Source

Escherichia Coli.

Formulation

The Mouse IL-33 was lyophilized from a sterile 0.2 micron filtered aqueous solution containing 10mM sodium phosphate, pH 7.5.

Purity

Greater than 90.0% as determined by analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of the proliferation of murine D10S cells is 0.04ng/ml, corresponding to a specific activity of 2.5x10⁷units/mg.

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Introduction
Interleukin 33 (IL-33) is a 32kDa proinflammatory cytokine that may also regulate gene transcription in producer cells. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1 (IL1 receptor-like-1), which is known also as ST2. Binding of IL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces expression of IL-4, IL-5, IL-13 and leads to severe pathological changes in mucosal organs and in vitro, it can be divided to N-terminal fragment of 12kDa and C-terminal fragment of 18kDa by cleavage of caspase-1.
Synonyms
Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, Il-33, Il1f11, 9230117N10Rik, Il33.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-33 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-33 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IL-33 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSIQGTSLLT QSPASLSTYN DQSVSFVLEN GCYVINVDDS GKDQEQDQVL LRYYESPCPA SQSGDGVDGK KLMVNMSPIK DTDIWLHAND KDYSVELQRG DVSPPEQAFF VLHKKSSDFV SFECKNLPGT YIGVKDNQLA LVEEKDESCN NIMFKLSKI.

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:

Killer Cell Lectin-Like Receptor Subfamily C, Member 2 Human Recombinant

Killer cell lectin-like receptor subfamily C member 2, NKG2-C type II integral membrane protein, NKG2-C-activating NK receptor, CD159 antigen-like family member C, NK cell receptor C, NKG2C, CD159c.

Product # :

PRO-1190

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Description

KLRC2 Human Recombinant produced in E. coli is a single polypeptide chain containing 162 amino acids (94-231) and having a molecular mass of 18.4 kDa.KLRC2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The KLRC2 solution (0.5mg/1ml) 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
KLRC2 has a part as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells. The group, designated KLRC (NKG2) are expressed mainly in natural killer (NK) cells and encodes a family of transmembrane proteins categorized by a type II membrane orientation (extracellular C terminus) and the presence of a C-type lectin domain. The KLRC (NKG2) gene family is situated inside the NK complex, a region which holds a few C-type lectin genes specially expressed on NK cells. KLRC2 alternative splice variants are known but their full-length nature is yet to be determined.
Synonyms
Killer cell lectin-like receptor subfamily C member 2, NKG2-C type II integral membrane protein, NKG2-C-activating NK receptor, CD159 antigen-like family member C, NK cell receptor C, NKG2C, CD159c.
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 MGSMIPFLEQ NNFSPNTRTQ KARHCGHCPE EWITYSNSCY YIGKERRTWE ESLLACTSKN SSLLSIDNEE EMKFLASILP SSWIGVFRNS SHHPWVTING LAFKHKIKDS DNAELNCAVL QVNRLKSAQC GSSMIYHCKH KL

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:

Activin-B Human Recombinant

Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

Product # :

CYT-058

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Description

Activin B human Recombinant produced in Nicotiana benthamiana plant is a beta-B single chain (aa 293-406) containing 123 amino acids (molecular formula C615H910N178O177S12). Activin B is fused to a 10-His-tag at the N-terminal having the total molecular mass of 14kDa and purified by standard chromatographic techniques.

Source

Nicotiana benthamiana plant

Formulation

Lyophilized from 1mg/ml solution in 0.05M Tris-HCl buffer pH 7.4.

Purity

Greater than 97.0% as determined by Analysis by SDS-PAGE.

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Introduction
Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.
Synonyms
Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Activin B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin B 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 Activin B in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG
Background
What is the molecular weight / Mw of Activin B Protein?
Activin A Protein has a total Mw of 14 kDa.

What is the source or expression system of Activin B Protein?
Nicotinia

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

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

What is the endotoxin level for Activin B Protein?
The endotoxin level is minimal, ACTIVIN B Protein was purified using conventional chromatography techniques.

What is the amino acid sequence of ACTIVIN B Protein?
HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

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

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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