Search: 1000 results found for "cntf"

Description:

Cytomegalo Virus Pp28 (UL99) Recombinant

Product # :

CMV-212

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Description

The E.Coli derived recombinant protein contains the CMV Pp28 (UL99) immunodominant regions, 130-160 amino acids.

Source

Escherichia Coli.

Formulation

50mM Tris-Hcl pH 7.2, 1mM EDTA and 50% glycerol.

Purity

CMV Pp28 protein is >95% pure as determined by 10% PAGE (coomassie staining).

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Introduction
The human cytomegalovirus UL99-encoded pp28 is a myristylated phosphoprotein that is a constituent of the virion. The pp28 protein is positioned within the tegument of the virus particle, a protein structure that resides between the capsid and envelope. In the infected cell, pp28 is found in a cytoplasmic compartment derived from the Golgi apparatus, where the virus buds into vesicles to acquire its final membrane.
Stability
CMV Pp28 protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Applications
CMV Pp28 antigen is suitable for ELISA and Western blots, excellent antigen for detection of CMV with minimal specificity problems.
Specificity
Immunoreactive with sera of CMV-infected individuals.
Purification Method
Purified by GS-4B Sepharose-Affinity Purification.

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:

Epidermal Growth Factor Rat Recombinant

Urogastrone, URG, EGF.

Product # :

CYT-669

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Description

Epidermal Growth Factor Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6151 Dalton. The Rat EGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Rat EGF was lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) 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 calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells is less than 0.1ng/ml, corresponding to a specific activity of > 10,000,000 units/mg.

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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Rat EGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat EGF 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 Rat EGF in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
NSNTGCPPSY DGYCLNGGVC MYVESVDRYV CNCVIGYIGE RCQHRDLRWW KLR.
Background
Pioneering Insights into Epidermal Growth Factor Rat Recombinant: Unraveling Signaling Dynamics and Therapeutic Implications
Abstract:
This research paper delves into the unexplored landscape of Epidermal Growth Factor Rat Recombinant (EGF-RR), delving into its intricate molecular attributes, signaling pathways, and potential therapeutic applications. By employing advanced methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the complex interplay between EGF-RR and cellular responses, offering a new perspective for therapeutic interventions.
Introduction:
Epidermal Growth Factor (EGF) holds a key role in cellular regulation. This paper navigates the intricacies of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and its potential therapeutic implications.
Protein Expression and Purification:
The paper delves into the meticulous engineering of EGF-RR, involving gene optimization for enhanced expression. Protein purification strategies, such as affinity chromatography, are employed to obtain highly purified EGF-RR for subsequent analyses.
Receptor Binding Assays and Ligand Interaction:
Advanced receptor binding assays elucidate the interaction of EGF-RR with its cognate receptor. By quantifying binding affinities and kinetic rates, the study unveils the nuances of EGF-RR's engagement with its receptor, shedding light on potential structural determinants.
Cellular Signaling Pathways and Functional Responses:
Through in vitro cellular assays, the study unravels the intricate signaling pathways initiated by EGF-RR. Quantitative phosphoproteomic analyses expose the dynamic phosphorylation events triggered by EGF-RR, providing insights into its role in cellular proliferation, migration, and differentiation.
Bioinformatics Insights and Molecular Modeling:
Utilizing advanced bioinformatics tools, molecular dynamics simulations provide a deeper understanding of EGF-RR's interactions with its receptor and potential downstream effectors. Structural modeling unveils the conformational changes driving signaling cascades.
Therapeutic Prospects and Novel Avenues:
The molecular insights into EGF-RR's signaling dynamics open avenues for therapeutic exploration. Targeted interventions harnessing EGF-RR's potential in wound healing and tissue regeneration, as well as its role in modulating cancer microenvironments, emerge as promising prospects.
Challenges and Future Directions:
Despite progress, challenges such as deciphering context-dependent signaling responses remain. Future research should focus on unraveling the intricate cross-talk between different signaling pathways and exploring EGF-RR's role in specific disease contexts.
Conclusion:
In a convergence of advanced methodologies and visionary insights, Epidermal Growth Factor Rat Recombinant emerges as a captivating subject. Its distinctive molecular attributes and complex cellular interplay offer potential avenues for therapeutic interventions, ushering in a new era of precision medicine.
What is the molecular weight/Mw of EGF RAT Protein?
EGF RAT Protein has a total Mw of 6.1kDa.

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

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

What is the Biological Activity of EGF RAT Protein?
The ED50 as calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells is less than 0.1ng/ml, corresponding to a specific activity of > 10,000,000 units/mg.

What is the amino acid sequence of EGF RAT Protein?
NSNTGCPPSY DGYCLNGGVC MYVESVDRYV CNCVIGYIGE RCQHRDLRWW KLR.

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

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

Cardiac Troponin-I Human

Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.

Product # :

PRO-2788

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Description

TNNI3 Native produced in Human heart tissue is a full length protein which has an additional amino acid residues on its N terminus that are not present on the skeletal form, making this protein a promising analyte for indicating cardiac specificity.TNNI3 Native is purified by proprietary chromatographic technique.

Source

Human heart tissue.

Formulation

TNNI3 was lyophilized from 0.01M HCl.

Purity

Greater than 98.0% as determined by SDS-PAGE.

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Synonyms
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Cardiac Troponin-I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNNI3 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 TNNI3 in Tris/urea buffer (20mM Tris, pH 7.5, 7M urea, 5mM EDTA, 15mM 2-mercaptoethanol) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
Troponin I, encoded by the TNNI3 gene, is a critical component of the troponin complex in cardiac muscle cells. It plays a central role in the regulation of cardiac muscle contraction by modulating the interaction between actin and myosin filaments.
While extensive research has been conducted on troponin I in the context of cardiac diseases, there is a growing need to investigate native human troponin I (TNNI3) in its unmodified form to gain a deeper understanding of its functions, structural significance, and implications for heart health. This research aims to provide a comprehensive exploration of TNNI3 in its native state, shedding light on its various roles and potential applications in cardiology and biomedical research.
The primary objective of this research is to elucidate the physiological role of native human TNNI3 in cardiac muscle contraction. Experiments involving human cardiac tissue samples and isolated myocytes will be conducted to investigate how TNNI3 interacts with other components of the troponin complex and influences calcium-mediated muscle contraction. Understanding these mechanisms is fundamental for deciphering the complexities of cardiac muscle physiology and its implications for heart health.
The second objective is to assess the clinical relevance of native TNNI3 in cardiac diseases. Clinical studies involving patients with various cardiac conditions will be conducted to evaluate the diagnostic and prognostic value of TNNI3 as a biomarker. These investigations may provide valuable insights into the use of native TNNI3 in the early detection and management of heart diseases.
The third objective is to explore the potential applications of native TNNI3 in biomedical research and drug development. Research will investigate the use of native TNNI3-expressing cells as models for studying cardiac disorders and for developing novel therapeutic interventions targeting the troponin complex.
By delving into the functions and roles of native human TNNI3, this research aims to expand our knowledge of cardiac muscle physiology, its implications for cardiac diseases, and its potential applications in cardiology and biomedical research.

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:

Cytomegalo Virus Pp38 (UL80a) Recombinant

Product # :

CMV-213

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Description

The E.Coli derived 52.8kDa recombinant protein contains the CMV Pp38 (UL80a) immunodominant regions, 117-373 amino acids and fused to a GST-Tag at C-terminus.

Source

Escherichia Coli.

Formulation

1mg/ml in 50mM Tris pH-7.2, 1mM EDTA and 50% glycerol.

Purity

CMV Pp38 protein is >95% pure as determined by 10% PAGE (coomassie staining).

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Introduction
CMV belongs to the Betaherpesvirinae subfamily of Herpesviridae which includes herpes simplex virustypes 1 and 2, varicella-zoster virus, and Epstein-Barrvirus. The herpesviruses share a characteristic ability to remain latentover long periods. CMV is a double-stranded linear DNA virus with 162 hexagonal protein capsomeres surrounded by a lipid membrane. CMV has the largest genome of the herpes viruses, ranging from 230-240 kilobase pairs. Human CMV is composed of unique and inverted repeats that include the existence of 4 genome isomers caused by inversion of L-S genome components (class E). Replication may be divided into immediate early, delayed early, and late gene expression based on time of synthesis after infection. The DNA is replicated by rolling circles. In vitro, CMV replicates in human fibroblasts.
Stability
CMV Pp38 Protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Purification Method
CMV Pp38 was purified by proprietary chromatographic technique.

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:

Nuclear Apoptosis Inducing Factor 1 Human Recombinant

bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.

Product # :

PRO-1978

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Description

NAIF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (1-327 a.a) and having a molecular mass of 37.6kDa. NAIF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

NAIF1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Nuclear Apoptosis Inducing Factor 1 (NAIF1) is a part of the NAIF1 family. NAIF1 Interacts with HARBI1 and Induces apoptosis.
Synonyms
bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.
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 MGSMAVPAKK RKMNFSEREV EIIVEELELK KHLLVNHFNA GVPLAAKSAA WHGILRRVNA VATCRRELPE VKKKWSDLKT EVRRKVAQVR AAVEGGEAPG PTEEDGAGGP GTGGGSGGGG PAVAPVLLTP MQQRICNLLG EATIISLPST TEIHPVALGP SATAAAATVT LTQIPTETTY HTLEEGVVEY CTAEAPPPLP PETPVDMMAQ HADTSVKPQA LKSRIALNSA KLIQEQRVTN LHVKEIAQHL EQQNDLLQMI RRSQEVQACA QERQAQAMEG TQAALSVLIQ VLRPMIKDFR RYLQSNTANP APASDPGQVA QNGQPDSIIQ.

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:

Nuclear Factor Erythroid 2-Like 2 Human Recombinant

NFE2L2, Nuclear factor erythroid 2-related factor 2, NF-E2-related factor 2, NFE2-related factor 2, HEBP1, Nuclear factor, erythroid derived 2, like 2, NRF2.

Product # :

PRO-2167

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Description

NFE2L2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 625 amino acids (1-605 a.a) and having a molecular mass of 69.9kDa.NFE2L2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

NFE2L2 protein solution (0.25mg/ml) in Phosphate buffer saline (pH 7.4) containing 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Nuclear factor (erythroid-derived 2)-like 2 (NRF2) is bZIP transcription factors which heterodimerize with Maf proteins to bind Mare sequences. In addition, the NRF proteins bind the antioxidant response element (ARE) and are associated with the regulation of detoxification enzymes and the oxidative stress response. NRF2 is extensively expressed and is assumed to translocate to the nucleus after treatment with xenobiotics and antioxidants, which stimulate its release from its repressor protein, Keap1.
Synonyms
NFE2L2, Nuclear factor erythroid 2-related factor 2, NF-E2-related factor 2, NFE2-related factor 2, HEBP1, Nuclear factor, erythroid derived 2, like 2, NRF2.
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 MMDLELPPPG LPSQQDMDLI DILWRQDIDL GVSREVFDFS QRRKEYELEK QKKLEKERQE QLQKEQEKAF FAQLQLDEET GEFLPIQPAQ HIQSETSGSA NYSQVAHIPK SDALYFDDCM QLLAQTFPFV DDNEVSSATF QSLVPDIPGH IESPVFIATN QAQSPETSVA QVAPVDLDGM QQDIEQVWEE LLSIPELQCL NIENDKLVET TMVPSPEAKL TEVDNYHFYS SIPSMEKEVG NCSPHFLNAF EDSFSSILST EDPNQLTVNS LNSDATVNTD FGDEFYSAFI AEPSISNSMP SPATLSHSLS ELLNGPIDVS DLSLCKAFNQ NHPESTAEFN DSDSGISLNT SPSVASPEHS VESSSYGDTL LGLSDSEVEE LDSAPGSVKQ NGPKTPVHSS GDMVQPLSPS QGQSTHVHDA QCENTPEKEL PVSPGHRKTP FTKDKHSSRL EAHLTRDELR AKALHIPFPV EKIINLPVVD FNEMMSKEQF NEAQLALIRD IRRRGKNKVA AQNCRKRKLE NIVELEQDLD HLKDEKEKLL KEKGENDKSL HLLKKQLSTL YLEVFSMLRD EDGKPYSPSE YSLQQTRDGN VFLVPKSKKP DVKKN.

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:

Chromosome 7 Open Reading Frame 49 Human Recombinant

MRI, Modulator of retrovirus infection homolog, C7orf49.

Product # :

PRO-1415

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Description

C7ORF49 Human Recombinant produced in E. coli is a single polypeptide chain containing 180 amino acids (1-157) and having a molecular mass of 19.2kDa. C7ORF49 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The C7ORF49 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Chromosome 7 Open Reading Frame 49 (C7ORF49) is affiliated with the lncRNA class. C7ORF49 characterizes the hamster ortholog and suggests that it may modulate the ability of the proteasome to degrade retroviral cores upon cellular infection.
Synonyms
MRI, Modulator of retrovirus infection homolog, C7orf49.
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 MGSMETLQSE TKTRVLPSWL TAQVATKNVA PMKAPKRMRM AAVPVAAARL PATRTVYCMN EAEIVDVALG ILIESRKQEK ACEQPALAGA DNPEHSPPCS VSPHTSSGSS SEEEDSGKQA LAPGLSPSQR PGGSSSACSR SPEEEEEEDV LKYVREIFFS.

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:

Protein O-Glucosyltransferase 1 Human Recombinant

POGLUT1, C3orf9, CLP46, hCLP46, KDELCL1, KTELC1, Protein O-glucosyltransferase 1, CAP10-like 46 kDa protein, KTEL motif-containing protein 1, Myelodysplastic syndromes relative protein, O-glucosyltransferase Rumi homolog, hRumi, Protein O-xylosyltransferase, MDSRP.

Product # :

ENZ-956

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Description

POGLUT1 Human Recombinant produced in in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 377 amino acids (24-392a.a) and having a molecular mass of 44.5kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). POGLUT1 is fused to a 8 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The POGLUT1 solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
POGLUT1 is a homologue of Rumi from Drosophila, an endoplasmic reticulum (ER)-retaining glucosyltransferase which catalyzes the transfer of glucose and xylose from UDP-glucose and UDP-xylose, respectively, to EGF repeats on the consensus sequence C-X-S-X-P-C. POGLUT1 positively regulates Notch signaling without affecting Notch ligand binding.
Synonyms
POGLUT1, C3orf9, CLP46, hCLP46, KDELCL1, KTELC1, Protein O-glucosyltransferase 1, CAP10-like 46 kDa protein, KTEL motif-containing protein 1, Myelodysplastic syndromes relative protein, O-glucosyltransferase Rumi homolog, hRumi, Protein O-xylosyltransferase, MDSRP.
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
RQKESGSKWK VFIDQINRSL ENYEPCSSQN CSCYHGVIEE DLTPFRGGIS RKMMAEVVRR KLGTHYQITK NRLYRENDCM FPSRCSGVEH FILEVIGRLP DMEMVINVRD YPQVPKWMEP AIPVFSFSKT SEYHDIMYPA WTFWEGGPAV WPIYPTGLGR WDLFREDLVR SAAQWPWKKK NSTAYFRGSR TSPERDPLIL LSRKNPKLVD AEYTKNQAWK SMKDTLGKPA AKDVHLVDHC KYKYLFNFRG VAASFRFKHL FLCGSLVFHV GDEWLEFFYP QLKPWVHYIP VKTDLSNVQE LLQFVKANDD VAQEIAERGS QFIRNHLQMD DITCYWENLL SEYSKFLSYN VTRRKGYDQI IPKMLKTELL EHHHHHH.

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:

Pigment Epithelium-Derived Factor Human Recombinant, HEK

Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

Product # :

CYT-553

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Description

PEDF Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain containing a total of 410 amino acids, having a molecular mass of 45.6 kDa and fused to an 11 aa FLAG tag at C-Terminus.The Human PEDF is purified by proprietary chromatographic techniques.

Source

HEK 293.

Formulation

The filtered (0.4µm) concentrated (0.5mg/ml) protein solution was lyophilized with 20mM Tris & 20mM NaCl pH-7.5.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
PEDF is a neurotrophic protein that induces extensive neuronal differentiation in retinoblastoma cells. SerpinF1 is a potent inhibitor of angiogenesis. EPC1 doesn’t undergo the stressed to relaxed conformation transition characteristic as of the active serpins since it exhibits no serine protease inhibitory activity.
Aqueous humour level of asymmetric dimethylarginine is correlated with PEDF in humans. ADMA and PEDF levels are increased in response to inflammation in uveitis.
Lack of PEDF expression is a potent factor for the enhancement of tumor growth and angiogenesis in breast cancer.
PEDF & VEGF genes contribute to the development of diabetic retinopathy.
PEDF and VEGF structural changes in blood vessel wall play an important role in the pathophysiology of PD patients.
PEDF-overexpressing tumors exhibited reduced intratumoral angiogenesis.
SerpinF1 is a new promising approach for the treatment of osteosarcoma.
Levels of the natural ocular anti-angiogenic factor SentrinF1 (PEDF) is associated with proliferative retinopathy.
VEGF secreted by retinal pigment epithelial cells upregulates PEDF expression via VEGFR-1 in an autocrine manner.
Sentrin-F1 concentration in the aqueous humor of diabetic patients predicts who will develop progression of retinopathy.
PEDF blocks angiogenic effects of leptin through its anti-oxidative properties.
Synonyms
Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
Solubility
It is recomnded to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
QNPASPPEEG SPDPDSTGAL VEEEDPFFKV PVNKLAAAVS NFGYDLYRVR SSTSPTTNVL LSPLSVATAL SALSLGAEQR TESIIHRALY YDLISSPDIH GTYKELLDTV TAPQKNLKSA SRIVFEKKLR IKSSFVAPLE KSYGTRPRVL TGNPRLDLQE INNWVQAQMK GKLARSTKEI PDEISILLLG VAHFKGQWVT KFDSRKTSLE DFYLDEERTV RVPMMSDPKA VLRYGLDSDL SCKIAQLPLT GSMSIIFFLP LKVTQNLTLI EESLTSEFIH DIDRELKTVQ AVLTVPKLKL SYEGEVTKSL QEMKLQSLFD SPDFSKITGK PIKLTQVEHR AGFEWNEDGA GTTPSPGLQP AHLTFPLDYH LNQPFIFVLR DTDTGALLFI GKILDPRGPAAADYKDDDDK.

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:

Transferrin Receptor Human Recombinant, Sf9

Transferrin Receptor, P90, T9, TR, Transferrin Receptor (P90, CD71), Transferrin Receptor Protein 1, CD71 Antigen, IMD46, CD71, TFR1.

Product # :

PRO-2587

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Description

TFRC produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 669 amino acids (101-760a.a.) and having a molecular mass of 74.9kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). TFRC is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
The Transferrin glycoproteins are responsible for the blood levels of free iron by binding to iron in the plasma. The transferrin molecules in humans are encoded by a gene called TF. Transferrin binds to iron in a tight but reversible way. The iron levels that binds to transferrin are very low in comparison to the total body iron, nonetheless, it is extremely vital iron levels with the greatest turnover rate.
Synonyms
Transferrin Receptor, P90, T9, TR, Transferrin Receptor (P90, CD71), Transferrin Receptor Protein 1, CD71 Antigen, IMD46, CD71, TFR1.
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
ADPLAGTESP VREEPGEDFP AARRLYWDDL KRKLSEKLDS TDFTGTIKLL NENSYVPREA GSQKDENLAL Recombinant Human TFRC Protein Catalog Number: ATGP3825 YVENQFREFK LSKVWRDQHFVKIQVKDSAQ NSVIIVDKNG RLVYLVENPG GYVAYSKAAT VTGKLVHANF GTKKDFEDLY TPVNGSIVIV RAGKITFAEK VANAESLNAI GVLIYMDQTK FPIVNAELSF FGHAHLGTGD PYTPGFPSFN HTQFPPSRSS GLPNIPVQTI SRAAAEKLFG NMEGDCPSDW KTDSTCRMVTSESKNVKLTV SNVLKEIKIL NIFGVIKGFV EPDHYVVVGA QRDAWGPGAA KSGVGTALLL KLAQMFSDMV LKDGFQPSRS IIFASWSAGD FGSVGATEWL EGYLSSLHLK AFTYINLDKA VLGTSNFKVS ASPLLYTLIE KTMQNVKHPV TGQFLYQDSN WASKVEKLTL DNAAFPFLAYSGIPAVSFCF CEDTDYPYLG TTMDTYKELI ERIPELNKVA RAAAEVAGQF VIKLTHDVEL NLDYERYNSQ LLSFVRDLNQ YRADIKEMGL SLQWLYSARG DFFRATSRLT TDFGNAEKTD RFVMKKLNDR VMRVEYHFLS PYVSPKESPF RHVFWGSGSH TLPALLENLK LRKQNNGAFNETLFRNQLAL ATWTIQGAAN ALSGDVWDID NEFHHHHHH.

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:

Placental Growth Factor Human Recombinant

PIGF, PGF, PLGF-1

Product # :

CYT-1193

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Description

PLGF Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 21-170) containing 160 amino acids and having a molecular mass of 18.3kDa.PLGF is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Placental Growth Factor (PLGF) which is a member of the VEGF sub-family, is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. PLGFmainly plays a role in trophoblast growth and differentiation and binds to receptor vegfr-1/flt1.
Synonyms
PIGF, PGF, PLGF-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
DGSMAVPPQQ WALSAGNGSS EVEVVPFQEV WGRSYCRALE RLVDVVSEYP SEVEHMFSPS CVSLLRCTGC CGDENLHCVP VETANVTMQL LKIRSGDRPS YVELTFSQHV RCECRPLREK MKPERRRPKG RGKRRREKQR PTDCHLCGDA VPRRHHHHHH

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:

Transferrin Human Recombinant, CHO

Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.

Product # :

PRO-2782

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Description

Recombinant Human Transferrin produced in CHO cells is a glycosylated, polypeptide chain containing having a molecular mass of 76 kDa. Human Transferrin has homologous C and N-terminal domains, each of which binds one ion of ferric iron.

Source

Chinese Hamster Ovary cells.

Formulation

Transferrin solution contains 0.05% NaN3 and PBS.

Purity

Protein is >95% pure as determined by 10% PAGE (coomassie staining).

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Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
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.
Applications
Immunoassay, cell culture.
Background
Human recombinant transferrin, a glycoprotein responsible for iron transport in the body, has gained increasing attention in the fields of biomedicine and health sciences. This multifaceted protein serves as an essential carrier of iron and is crucial for cellular growth, immunity, and various physiological processes. Its recombinant form, produced through advanced biotechnological methods, offers several advantages for therapeutic and research purposes. This study aims to provide a comprehensive exploration of human recombinant transferrin, shedding light on its various functions and potential applications in health and biomedicine.
The primary objective of this research is to elucidate the essential role of transferrin in iron homeostasis and its significance for human health. In vitro and in vivo experiments will be conducted to investigate how recombinant transferrin interacts with cellular receptors, regulates iron uptake, and influences cellular proliferation. Understanding these mechanisms is fundamental for deciphering the complexities of iron metabolism and its impact on health and disease.
The second objective is to assess the clinical relevance of human recombinant transferrin in medical interventions. Clinical trials and studies involving individuals with iron-related disorders, such as iron-deficiency anemia, will be conducted to evaluate the efficacy and safety of recombinant transferrin supplementation. These investigations may provide insights into the use of recombinant transferrin as a therapeutic agent in various clinical settings.
The third objective is to explore the broader implications of human recombinant transferrin in biomedicine and research. Research will investigate its potential roles in areas beyond iron transport, such as drug delivery, tissue engineering, and cell culture. Understanding the multifaceted properties of recombinant transferrin may open new avenues for innovative approaches in various medical specialties and scientific research.
By delving into the diverse functions of human recombinant transferrin, this research aims to expand our understanding of its physiological roles and clinical applications. The findings may contribute to the development of innovative strategies for the treatment of iron-related disorders and the advancement of biomedicine and scientific research.

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 Migration Inhibitory Factor Human, Recombinant His Tag N-Terminus

Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.

Product # :

CYT-431

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Description

MIF human Recombinant, fused to 40 a.a. His-tag at N-terminus, was cloned into an E. coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques. Macrophage Inducing Factor Human Recombinant ( 1-115 a.a. ) is a single, non-glycosylated, polypeptide chain having a total amino acids of 155 and molecular mass of 17kDa.

Source

Escherichia Coli.

Formulation

1mg/ml solution containing PBS pH-7.4.

Purity

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

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Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
Synonyms
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
Physical Appearance
Sterile filtered colorless solution.
Stability
Liquid MIF although stable 4°C for 1 week, should be stored below -18°C. Please prevent freeze-thaw cycles.
Amino Acid Sequence
MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSMPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC LHSIGKIGGA QNRSYSKLLC GLLAERLRIS PDRVYINYYD MNAANVGWNN STFA.

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:

Cathepsin-S Mouse Recombinant

Cathepsin S, Ctss, Cats.

Product # :

ENZ-954

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Description

CTSS Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 325 amino acids (24-340 a.a.) and having a molecular mass of 36.9kDa.CTSS is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

CTSS protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Cathepsin S (CTSS) belongs to the peptidase C1 family. CTSS is a lysosomal cysteine proteinase that participates in the degradation of antigenic proteins to peptides for presentation on MHC class II molecules. CTSS functions as an elastase over a broad pH range in alveolar macrophages.
Synonyms
Cathepsin S, Ctss, Cats.
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
EQLQRDP TLDYHWDLWK KTHEKEYKDK NEEEVRRLIW EKNLKFIMIH NLEYSMGMHT YQVGMNDMGD MTNEEISCRM GALRISRQSP KTVTFRSYSN RTLPDTVDWR EKGCVTEVKY QGSCGACWAF SAVGALEGQL KLKTGKLISL SAQNLVDCSN EEKYGNKGCG GGYMTEAFQY IIDNGGIEAD ASYPYKAMDE KCHYNSKNRA ATCSRYIQLP FGDEDALKEA VATKGPVSVG IDASHSSFFF YKSGVYDDPS CTGNVNHGVL VVGYGTLDGK DYWLVKNSWG LNFGDQGYIR MARNNKNHCG IASYCSYPEI LEHHHHHHDY WLVKNSWGLN FGDQGYIRMA RNNKNHCGIA
SYCSYPEILE HHHHHH.

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

Description:

Interleukin-1 alpha Rat Recombinant

Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.

Product # :

CYT-381

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Description

Interleukin-1A Rat Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 155 amino acids and having a molecular mass of 17703 Dalton. The IL-1A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 50mM Tris-HCl, pH=8.

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 the dose-dependant stimulation of murine D10S cells is < 0.005 ng/ml, corresponding to a Specific Activity of 200,000,000IU/mg.

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Introduction
Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.
Synonyms
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A 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 1a 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 Ala-Pro-His-Ser-Phe.

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:

Lecithin-Cholesterol Acyltransferase Human Recombinant, HEK

Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.

Product # :

ENZ-254

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Description

LCAT Human Recombinant produced in HEK is a single, glycosylated, polypeptide chain containing 429 amino acids (25-440) which includes a 13 amino acid Flag Tag fused at N-terminus and having a total molecular mass of 48.5 kDa. LCAT Human Recombinant is purified by proprietary chromatographic techniques.

Source

Human Embryonic Kidney 293 cells

Formulation

The LCAT protein was lyophilized from 0.4um filtered solution at a concentration of 0.5mg/ml containing 20mM Tris buffer, and 50mM NaCl, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
LCAT is an extracellular cholesterol esterifying enzyme, lecithin-cholesterol acyltransferase. The esterification of cholesterol is required for cholesterol transport. LCAT is a essential enzyme in the extracellular metabolism of plasma lipoproteins.
Synonyms
Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized LCAT although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LCAT should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. LCAT HEK is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
HVDYKDDDDK PAGFWLLNVL FPPHTTPKAE LSNHTRPVIL VPGCLGNQLE AKLDKPDVVN WMCYRKTEDF FTIWLDLNMF LPLGVDCWID NTRVVYNRSS GLVSNAPGVQ IRVPGFGKTY SVEYLDSSKL AGYLHTLVQN LVNNGYVRDE TVRAAPYDWR LEPGQQEEYY RKLAGLVEEM HAAYGKPVFL IGHSLGCLHL LYFLLRQPQA WKDRFIDGFI SLGAPWGGSI KPMLVLASGD NQGIPIMSSI KLKEEQRITT TSPWMFPSRM AWPEDHVFIS TPSFNYTGRD FQRFFADLHF EEGWYMWLQS RDLLAGLPAP GVEVYCLYGV GLPTPRTYIY DHGFPYTDPV GVLYEDGDDT VATRSTELCG LWQGRQPQPV HLLPLHGIQH LNMVFSNLTL EHINAILLGA YRQGPPASPT ASPEPPPPE

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:

Vascular Endothelial Growth Factor D Human Recombinant

c-fos induced growth factor (vascular endothelial growth factor D), FIGF, VEGFD.

Product # :

CYT-045

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Description

VEGFD Human Recombinant produced in HEK-293 cells is a secreted protein (amino acids Phe93-Ser201) fused to a polyhistidine tag at the C-terminus.

Source

HEK293.

Formulation

The recombinant VEGF-D was lyophilized after extensive dialysis against PBS.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 of 3-4ng/ml is measured by its ability to stimulate the proliferation of human microvascular endothelial cells (HMVECs).

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Introduction
VEGF-D belongs to the VEGF/PDGF family of proteins. VEGF-D promotes lymphangiogesis, endothelial cell growth, and regulates vascular permeability. In addition, VEGF-D has an important part in the creation of the venous and lymphatic vascular systems and in the growth and maintenance of differentiated lymphatic endothelium Mature VEGF-D forms a noncovalently linked homodimer, and binds to and activate both VEGFR-2 (flk1) and VEGFR-3 (flt4).
Synonyms
c-fos induced growth factor (vascular endothelial growth factor D), FIGF, VEGFD.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized VEGF-D although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-D 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 Vascular Endothelial Growth Factor D in sterile 18M-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

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

Description:

Growth and Differentiation factor 7 Mouse Recombinant

Growth/differentiation factor 7, GDF-7, Gdf7.

Product # :

CYT-946

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Description

GDF7 Mouse Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 146 amino acids and having a molecular mass of 29.8kDa.The GDF-7 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GDF7 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

Purity

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

Biological Activity

The ED₅₀ as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 0.5µg/ml, corresponding to a specific activity of > 2000 IU/mg.

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Introduction
Growth Differentiation Factor-7 (GDF-7) belongs to the BMP family of TGF-b superfamily proteins. GDF7 elicits its bioactivity via a heterodimeric receptor complex comprised of a type 1 (BMPR-IB) and a type II (BMPR-II or Activin RII) serine/threonine kinase receptor. GDF7 signaling results in the phosphorylation and activation of Smad proteins. GDF-7 is also involved in tendon and ligament formation and repair. In addition, GDF7 regulates bone formation, mesenchymal stem cell differentiation, neuronal differentiation, and axon guidance.
Synonyms
Growth/differentiation factor 7, GDF-7, Gdf7.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GDF7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF-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 GDF-7 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TALAGTRGAQ GSGGGGGGGG GGGGGGGGGG GGAGRGHGRR GRSRCSRKSL HVDFKELGWD DWIIAPLDYE AYHCEGVCDF PLRSHLEPTN HAIIQTLLNS MAPDAAPASC CVPARLSPIS ILYIDAANNV VYKQYEDMVV EACGCR.
Background
What is the molecular weight/Mw of GDF7 Protein?
GDF7 Protein has a total Mw of 29.8kDa.

What is the source or expression system of GDF7 Protein?
Escherichia Coli.

What is the Purity of GDF7 Protein?
GDF7 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF7 Protein?
The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 0.5µg/ml, corresponding to a specific activity of > 2000 IU/mg.

What is the amino acid sequence of GDF7 Protein?
TALAGTRGAQ GSGGGGGGGG GGGGGGGGGG GGAGRGHGRR GRSRCSRKSL HVDFKELGWD DWIIAPLDYE AYHCEGVCDF PLRSHLEPTN HAIIQTLLNS MAPDAAPASC CVPARLSPIS ILYIDAANNV VYKQYEDMVV EACGCR.

What applications can GDF7 Protein be used in?
GDF7 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF7 Protein?
The endotoxin level is minimal, GDF7 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 4 Human Recombinant, Yeast

BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.

Product # :

CYT-712

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Description

Interleukin-4 Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 129 amino acids.The IL-4 is purified by proprietary chromatographic techniques.

Source

Pichia pastoris.

Formulation

The protein was lyophilized from 0.2µm filtered solution in 20mM sodium phosphate buffer pH 6.0 in absence of any carrier protein.

Purity

Greater than 98% as determined by SDS-PAGE.

Biological Activity

The biological activity is determined by measuring the dose-dependent proliferation of human TF–1 cells and CD23 expression. A concentration range of 0.1–10.0 ng/ml is effective for most in vitro applications. ED₅₀ = 0.05–0.4ng/ml.

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Introduction
IL4 is a pleiotropic cytokine produced by activated T cells. IL4 is a ligand for interleukin 4 receptor. The interleukin 4 receptor also binds to IL13, which may contribute to many overlapping functions of this cytokine and IL13. STAT6, a signal transducer and activator of transcription, has been shown to play a central role in mediating the immune regulatory signal of this cytokine. This gene, IL3, IL5, IL13, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL13. IL4, IL13 and IL5 are found to be regulated coordinately by several long-range regulatory elements in an over 120 kilobase range on the chromosome. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.
Synonyms
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Interleukin-4 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 Interleukin-4 in sterile 18M-cm H2O 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:

Vascular Endothelial Growth Factor Human Recombinant, His

Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

Product # :

CYT-496

Price :

Quantity :

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Description

Vascular Endothelial Growth Factor Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain (aa 207-371) containing a total of 185 amino acids and having a molecular mass of 21.3 kDa (corresponding to Isoform L-VEGF165 UniProt acc#P15692-11). The VEGF is fused to a 20 a.a His-tag at N-terminus and is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

VEGF His (0.5mg/ml) is supplied in 20mM Tris-HCl pH-8.5, 50% glycerol, 5mM DTT, 200mM NaCl & 2mM EDTA.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
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 APMAEGGGQN HHEVVKFMDV YQRSYCHPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TEESNITMQI MRIKPHQGQH IGEMSFLQHN KCECRPKKDR ARQENPCGPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR.

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 20 Human Recombinant

Keratin type I cytoskeletal 20, Cytokeratin-20, CK-20, Keratin-20, K20, Protein IT, KRT20, CD20, CK20, KRT21, MGC35423.

Product # :

PRO-351

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Quantity :

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source
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Description

Cytokeratin 20 Human Recombinant produced in E.Coli is a single,non-glycosylated polypeptide chain having a molecular mass of 48,553 Dalton. The KRT20 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
KRT20 is a member of the keratin family. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins consist of acidic proteins which are arranged in pairs of heterotypic keratin chains. This cytokeratin is a major cellular protein of mature enterocytes and goblet cells and is specifically expressed in the gastric and intestinal mucosa. The type I cytokeratin genes are clustered in a region of chromosome 17q12-q21.
Synonyms
Keratin type I cytoskeletal 20, Cytokeratin-20, CK-20, Keratin-20, K20, Protein IT, KRT20, CD20, CK20, KRT21, MGC35423.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized KRT20 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution KRT20 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 KRT20 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 9.5 M urea buffer (see above). Protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4 M urea and then to low salt condition (50 mM NaCI, 2 mM dithiothreitol, 10 mM 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:

Natriuretic Peptide C Human Recombinant

Natriuretic Peptide Precursor C, C-Type Natriuretic Peptide, CNP2, CNP.

Product # :

CYT-760

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Description

NPPC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (24-126) and having a molecular mass of 13.2kDa.NPPC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The NPPC solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
NPPC is proteolytically managed to create a secreted hormone of the natriuretic peptide family. NPPC is vasoactive and natriuretic and controls the evolution and differentiation of cartilaginous growth plate chondrocytes.
Synonyms
Natriuretic Peptide Precursor C, C-Type Natriuretic Peptide, CNP2, CNP.
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 MGSKPGAPPK VPRTPPAEEL AEPQAAGGGQ KKGDKAPGGG GANLKGDRSR LLRDLRVDTK SRAAWARLLQ EHPNARKYKG ANKKGLSKGC FGLKLDRIGS MSGLGC

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:

Allograft Inflammatory Factor 1 Human Recombinant

AIF-1, Allograft inflammatory factor 1, Em:AF129756.17, G1, IBA1, Ionized calcium-binding adapter molecule 1, IRT-1, Protein G1, AIF1.

Product # :

CYT-697

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Description

AIF1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (1-147a.a.) and having a molecular mass of 18.9kDa. AIF1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E. Coli.

Formulation

The AIF1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
2mM DTT, 200mM NaCl and 20% glycerol.

Purity

Greater than 95% as determined by SDS PAGE.

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Introduction
Human AIF1 protein shares 98% homology/identity with that of rat. AIF1 is expressed in macrophages and neutrophils. The expression of AIF1 transcripts is upregulated by IFN-g in rat macrophages. AIF1 is expressed selectively in human macrophage-like cell lines, and in a subset of CD68(+) macrophages in the interstitial and perivascular spaces of human heart allografts. In quiescent cultured human vascular smooth muscle cells synthesis of AIF1 is induced by IFN-g, IL1b, and conditioned medium of T-cells. Overexpression of AIF1 in human VSMCs results in enhanced growth of these cells. AIF1 is expressed during apoptosis rat mammary gland and ventral prostate tissues. Allograft Inflammatory Factor 1 is expressed by several tumor-associated activated macrophages and microglial cells in rat and human gliomas. There is an evident relationship of AIF1-expressing activated macrophages and microglial cells with tumor malignancy in humans.
Synonyms
AIF-1, Allograft inflammatory factor 1, Em:AF129756.17, G1, IBA1, Ionized calcium-binding adapter molecule 1, IRT-1, Protein G1, AIF1.
Stability
Store AIF1 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 MSQTRDLQGG KAFGLLKAQQ EERLDEINKQ FLDDPKYSSD EDLPSKLEGF KEKYMEFDLN GNGDIDIMSL KRMLEKLGVP KTHLELKKLI GEVSSGSGET FSYPDFLRMM LGKRSAILKM ILMYEEKARE KEKPTGPPAK KAISELP.
Background
Allograft Inflammatory Factor 1 Human Recombinant: Uncovering its Role in Immune Responses and Therapeutic Prospects
1. Abstract
This paper explores the Allograft Inflammatory Factor 1 Human Recombinant (AIF-1), a cytoplasmic, IFN-gamma-inducible calcium-binding protein involved in inflammation and immunity. We review the structure, biological roles, and involvement of AIF-1 in disease pathology. The therapeutic potential of AIF-1 in immune-related disorders is also explored.
2. Introduction
AIF-1, also known as IBA1, plays an important role in immune responses. It is associated with various immune cells, particularly macrophages, and has been implicated in numerous inflammatory and immune-related diseases. Understanding the function of AIF-1 could aid the development of novel therapeutic strategies.
3. Structure and Signaling of AIF-1
AIF-1 is a small 17 kDa protein with an EF-hand calcium-binding motif. Although the precise mechanism by which AIF-1 exerts its functions is not entirely clear, it is known to regulate the activation, migration, and proliferation of macrophages, key cells involved in immune responses.
4. Biological Functions of AIF-1
AIF-1 has been shown to play key roles in macrophage activation and function, which are central to inflammation and immunity. It is also implicated in cell survival, proliferation, and differentiation.
5. AIF-1 in Disease Pathology
AIF-1 has been associated with a range of inflammatory and immune-related diseases, including rheumatoid arthritis, atherosclerosis, and multiple sclerosis. It is also implicated in several cancers, further underscoring its broad physiological and pathological relevance.
6. Therapeutic Potential of AIF-1
Given its pivotal role in immune responses, AIF-1 presents an intriguing target for therapeutic interventions in immune-related diseases. Modulating the activity of AIF-1 could potentially alleviate pathological inflammation and autoimmunity.
7. Conclusion and Future Perspectives
Our knowledge of AIF-1 and its functions has significantly improved in recent years, but much remains to be discovered. Further research into AIF-1's exact molecular mechanisms and roles in disease will undoubtedly contribute to the development of novel therapeutic strategies.
What is the molecular weight/Mw of AIF1 Protein?
AIF1 Protein has a total Mw of 18.9kDa.

What is the source or expression system of AIF1 Protein?
Escherichia Coli.

What is the Purity of AIF1 Protein?
AIF1 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of AIF1 Protein?
The biological functionality of AIF1 Protein will be determined in the future.

What is the amino acid sequence of AIF1 Protein?
MGSSHHHHHH SSGLVPRGSH MSQTRDLQGG KAFGLLKAQQ EERLDEINKQ FLDDPKYSSD EDLPSKLEGF KEKYMEFDLN GNGDIDIMSL KRMLEKLGVP KTHLELKKLI GEVSSGSGET FSYPDFLRMM LGKRSAILKM ILMYEEKARE KEKPTGPPAK KAISELP.

What applications can AIF1 Protein be used in?
AIF1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for AIF1 Protein?
The endotoxin level is minimal, AIF1 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:

Heparan Sulfate 3-O-Sulfotransferase 1 Human Recombinant

Heparan sulfate glucosamine 3-O-sulfotransferase 1, Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 1, 3-OST-1, Heparan sulfate 3-O-sulfotransferase 1, h3-OST-1, HS3ST1, 3OST, 3OST1, HS3S1.

Product # :

ENZ-744

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Description

HS3ST1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 310 amino acids (21-307 a.a) and having a molecular mass of 36.2kDa.HS3ST1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HS3ST1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 2mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Heparan Sulfate 3-O-Sulfotransferase 1 (HS3ST1), is sulfotransferase which uses 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan. HS3ST1 catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact). This modification is a vital part in the biosynthesis of anticoagulant heparan sulfate since it concludes the structure of the antithrombin pentasaccharide binding site.
Synonyms
Heparan sulfate glucosamine 3-O-sulfotransferase 1, Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 1, 3-OST-1, Heparan sulfate 3-O-sulfotransferase 1,
h3-OST-1, HS3ST1, 3OST, 3OST1, HS3S1.
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 MGSRPAELGQ QELLRKAGTL QDDVRDGVAP NGSAQQLPQT IIIGVRKGGT RALLEMLSLH PDVAAAENEV HFFDWEEHYS HGLGWYLSQM PFSWPHQLTV EKTPAYFTSP KVPERVYSMN PSIRLLLILR DPSERVLSDY TQVFYNHMQK HKPYPSIEEF LVRDGRLNVD YKALNRSLYH VHMQNWLRFF PLRHIHIVDG DRLIRDPFPE IQKVERFLKL SPQINASNFY FNKTKGFYCL RDSGRDRCLH ESKGRAHPQV DPKLLNKLHE YFHEPNKKFF ELVGRTFDWH.

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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